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Conserved domains on  [gi|2217327184|ref|XP_047299966|]
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RUN and FYVE domain-containing protein 4 isoform X5 [Homo sapiens]

Protein Classification

RUN domain-containing protein( domain architecture ID 1908546)

RUN (RPIP8, unc-14 and NESCA) domain-containing protein may be involved in Ras-like GTPase signaling; similar to vertebrate RUN domain-containing protein 3A/3B that is Rap2-interacting protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RUN super family cl45896
RUN domain; RUN domain, named after RPIP8 (Rap2 interacting protein 8), UNC-14 and NESCA (new ...
 12-162 6.38e-87

RUN domain; RUN domain, named after RPIP8 (Rap2 interacting protein 8), UNC-14 and NESCA (new molecule containing SH3 at the carboxyl-terminus), is a less conserved protein motif that comprises six conserved regions, which in some proteins have considerable insertions between them. The domain core is thought to take up a predominantly alpha fold, with basic amino acids in regions A and D possibly playing a functional role in interactions with Ras GTPases. RUN domains are often found in proteins linked particularly to the functions of GTPases in the Rap and Rab families, suggesting the RUN domain may be involved in Rab-mediated membrane trafficking, possibly as a Rab-binding site. RUN domain-containing proteins could hence play important roles in multiple Ras-like GTPase signalling pathways.


The actual alignment was detected with superfamily member cd17697:

Pssm-ID: 459241  Cd Length: 150  Bit Score: 264.74  E-value: 6.38e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327184  12 KDLraAAVSAILQGYGDGQG-PVTDTSAELHRLCGCLELLLQFDQKEQKSFLGPRKDYWDFLCTALRRQRGNMEPIHFVR 90
Cdd:cd17697     1 KDL--QASIAELQKDQEEQQlPITDGSPELHRLCARLEYLLQFDQKEKKSFFGSRKDYWDFLCLCLNRHRGGTEGIHFVN 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217327184  91 SQDKLKTPLGKGRAFIRFCLARGQLAEALQLCLLNSELTREWYGPRSPLLCPERQEDILDSLYALNGVAFEL 162
Cdd:cd17697    79 STDKLKTPLGKGRAFIRYCLVQQQLAESLQLCLLNPELTGEWYYARSPFLSPELRSDILDSLYELNGVNFDL 150
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 402-514 1.28e-07

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


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.56  E-value: 1.28e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327184 402 ARREEQAEVS-LQDEIKSLRLGLRKAEEQAQRQEQLLREQEGELQALREQLSRCQEERAELQAQLEQKQQEAERRDAMYQ 480
Cdd:COG1196   289 EEYELLAELArLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALL 368

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2217327184 481 EELGGQRDLVQAMKRRVLELIQEKDRLWQRLQHL 514
Cdd:COG1196   369 EAEAELAEAEEELEELAEELLEALRAAAELAAQL 402
 
Name Accession Description Interval E-value
RUN_RUFY4 cd17697
RUN domain found in RUN and FYVE domain-containing protein 4 (RUFY4) and similar proteins; ...
 12-162 6.38e-87

RUN domain found in RUN and FYVE domain-containing protein 4 (RUFY4) and similar proteins; RUFY4 acts as a positive regulator that enhances autophagy and lysosome tethering in response to Interleukin-4. It is expressed in a cell-specific manner or under specific immunological conditions associated with IL4 expression such as allergic asthma. RUFY4 belongs to the FUFY protein family which is characterized by the presence of an N-terminal RUN domain and a C-terminal FYVE domain; this model represents the RUN domain of RUFY4.


Pssm-ID: 439059  Cd Length: 150  Bit Score: 264.74  E-value: 6.38e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327184  12 KDLraAAVSAILQGYGDGQG-PVTDTSAELHRLCGCLELLLQFDQKEQKSFLGPRKDYWDFLCTALRRQRGNMEPIHFVR 90
Cdd:cd17697     1 KDL--QASIAELQKDQEEQQlPITDGSPELHRLCARLEYLLQFDQKEKKSFFGSRKDYWDFLCLCLNRHRGGTEGIHFVN 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217327184  91 SQDKLKTPLGKGRAFIRFCLARGQLAEALQLCLLNSELTREWYGPRSPLLCPERQEDILDSLYALNGVAFEL 162
Cdd:cd17697    79 STDKLKTPLGKGRAFIRYCLVQQQLAESLQLCLLNPELTGEWYYARSPFLSPELRSDILDSLYELNGVNFDL 150
RUN pfam02759
RUN domain; This domain is present in several proteins that are linked to the functions of ...
 42-164 9.00e-09

RUN domain; This domain is present in several proteins that are linked to the functions of GTPases in the Rap and Rab families. They could hence play important roles in multiple Ras-like GTPase signalling pathways. The domain is comprises six conserved regions, which in some proteins have considerable insertions between them. The domain core is thought to take up a predominantly alpha fold, with basic amino acids in regions A and D possibly playing a functional role in interactions with Ras GTPases.


Pssm-ID: 460679  Cd Length: 134  Bit Score: 53.82  E-value: 9.00e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327184  42 RLCGCLELLLQ------FDQKEQKSFLGPRKDYWDFL------CTA---LRRQRGNMEPIHfvrsqdKLKTPLGKGRAFI 106
Cdd:pfam02759   1 QLCAALEALLShglkrsSLLILRAAGLLPERSFWALLervgklVPPaeeLLSSVQELEQIH------TPYSPDGRGRAWI 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2217327184 107 RFCLARGQLAEALQLCLLNSELTREWYGPRSPLLCPERQEDILDSLYALNGVAFELDL 164
Cdd:pfam02759  75 RLALNEKLLDQWLKLLLSNKELLSEYYEPWALLADPEFGEILLGLLVGLSALDFNLCL 132
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 402-514 1.28e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.56  E-value: 1.28e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327184 402 ARREEQAEVS-LQDEIKSLRLGLRKAEEQAQRQEQLLREQEGELQALREQLSRCQEERAELQAQLEQKQQEAERRDAMYQ 480
Cdd:COG1196   289 EEYELLAELArLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALL 368

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2217327184 481 EELGGQRDLVQAMKRRVLELIQEKDRLWQRLQHL 514
Cdd:COG1196   369 EAEAELAEAEEELEELAEELLEALRAAAELAAQL 402
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 398-517 5.87e-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: 49.28  E-value: 5.87e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327184  398 VTLVARREEQAEVsLQDEIKSLRLGLRKAEEQAQRQEQLLREQEGELQALREQLSRCQEERAELQAQLE---QKQQEAER 474
Cdd:TIGR02168  294 ANEISRLEQQKQI-LRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEeleAELEELES 372

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 2217327184  475 RDAMYQEELGGQRDLVQAMKRRVLELIQEKDRLWQRLQHLSSM 517
Cdd:TIGR02168  373 RLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDR 415
RUN smart00593
domain involved in Ras-like GTPase signaling;
102-164 1.14e-05

domain involved in Ras-like GTPase signaling;


Pssm-ID: 214736 [Multi-domain]  Cd Length: 64  Bit Score: 42.99  E-value: 1.14e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217327184  102 GRAFIRFCLARGQLAEALQLCLLNSELTREWYGPRSPLLCPERQEDILDSLYALNGVAFELDL 164
Cdd:smart00593   1 FRAWIRLALNEKLLSSWLNLLLSDEELLSKYYEPWAFLRDPEEGEQLLGLLVGLSALDFNLPV 63
hsdR PRK11448
type I restriction enzyme EcoKI subunit R; Provisional
 406-506 2.64e-05

type I restriction enzyme EcoKI subunit R; Provisional


Pssm-ID: 236912 [Multi-domain]  Cd Length: 1123  Bit Score: 47.25  E-value: 2.64e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327184  406 EQAEVSLQDEIKSLRLGLRKAEEQAQRQEQLLREQEGELQALREQLSRCQEERAELQAQLEQKQQEAERRDAMYQEELGG 485
Cdd:PRK11448   141 ENLLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAETSQERKQKRKE 220

                           90       100
                   ....*....|....*....|.
gi 2217327184  486 QRDlvQAMKRrvLELIQEKDR 506
Cdd:PRK11448   221 ITD--QAAKR--LELSEEETR 237
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 393-499 3.75e-05

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 46.65  E-value: 3.75e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327184  393 QVQTEVTLVARR----EEQAEVSLQDEIKSLRLGLRKAEEqaqRQEQLLREQEGELQALREQLSRCQEERAELQAQLEQK 468
Cdd:pfam15921  228 ELDTEISYLKGRifpvEDQLEALKSESQNKIELLLQQHQD---RIEQLISEHEVEITGLTEKASSARSQANSIQSQLEII 304

                           90       100       110
                   ....*....|....*....|....*....|.
gi 2217327184  469 QQEAERRDAMYQEELGGQRDLVQAMKRRVLE 499
Cdd:pfam15921  305 QEQARNQNSMYMRQLSDLESTVSQLRSELRE 335
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 425-503 4.97e-04

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 214922 [Multi-domain]  Cd Length: 140  Bit Score: 40.26  E-value: 4.97e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327184  425 KAEEQAQRQEQLLREQEGELQALREQLSR-----CQEERAELQAQLEQKQQEAERRDAMYQEEL-GGQRDLVQAMKRRVL 498
Cdd:smart00935  22 QLEKEFKKRQAELEKLEKELQKLKEKLQKdaatlSEAAREKKEKELQKKVQEFQRKQQKLQQDLqKRQQEELQKILDKIN 101


                   ....*
gi 2217327184  499 ELIQE 503
Cdd:smart00935 102 KAIKE 106
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 407-504 1.93e-03

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


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 40.25  E-value: 1.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327184 407 QAEVSLQDEIKSLRLgLRKAEEQAQRQEQLLREQEGELQALREQLSRCQEERAE-LQAQLEQKQQEAERR-DAMYQEELG 484
Cdd:cd16269   188 QADQALTEKEKEIEA-ERAKAEAAEQERKLLEEQQRELEQKLEDQERSYEEHLRqLKEKMEEERENLLKEqERALESKLK 266

                          90       100
                  ....*....|....*....|
gi 2217327184 485 GQRDLVQAMKRRVLELIQEK 504
Cdd:cd16269   267 EQEALLEEGFKEQAELLQEE 286
 
Name Accession Description Interval E-value
RUN_RUFY4 cd17697
RUN domain found in RUN and FYVE domain-containing protein 4 (RUFY4) and similar proteins; ...
 12-162 6.38e-87

RUN domain found in RUN and FYVE domain-containing protein 4 (RUFY4) and similar proteins; RUFY4 acts as a positive regulator that enhances autophagy and lysosome tethering in response to Interleukin-4. It is expressed in a cell-specific manner or under specific immunological conditions associated with IL4 expression such as allergic asthma. RUFY4 belongs to the FUFY protein family which is characterized by the presence of an N-terminal RUN domain and a C-terminal FYVE domain; this model represents the RUN domain of RUFY4.


Pssm-ID: 439059  Cd Length: 150  Bit Score: 264.74  E-value: 6.38e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327184  12 KDLraAAVSAILQGYGDGQG-PVTDTSAELHRLCGCLELLLQFDQKEQKSFLGPRKDYWDFLCTALRRQRGNMEPIHFVR 90
Cdd:cd17697     1 KDL--QASIAELQKDQEEQQlPITDGSPELHRLCARLEYLLQFDQKEKKSFFGSRKDYWDFLCLCLNRHRGGTEGIHFVN 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217327184  91 SQDKLKTPLGKGRAFIRFCLARGQLAEALQLCLLNSELTREWYGPRSPLLCPERQEDILDSLYALNGVAFEL 162
Cdd:cd17697    79 STDKLKTPLGKGRAFIRYCLVQQQLAESLQLCLLNPELTGEWYYARSPFLSPELRSDILDSLYELNGVNFDL 150
RUN_FYCO1 cd17698
RUN domain found in FYVE and coiled-coil domain-containing protein 1 (FYCO1) and similar ...
 9-162 1.81e-53

RUN domain found in FYVE and coiled-coil domain-containing protein 1 (FYCO1) and similar proteins; FYCO1, also called zinc finger FYVE domain-containing protein 7 (ZFYVE7), is a multidomain autophagy adaptor protein that interacts with kinesin motor proteins and with the autophagosomal membrane components microtubule-associated protein 1 light chain 3 (LC3), Rab7, and Phosphatidylinositol 3-phosphate (PI3P), to mediate microtubule plus-end-directed autophagosome transport. This model represents the RUN domain of FYCO1.


Pssm-ID: 439060  Cd Length: 158  Bit Score: 178.35  E-value: 1.81e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327184   9 KVTKDLRAAaVSAILQGYGDGQGPVTDTSAELHRLCGCLELLLQFDQKEQKSFLGPRKDYWDFLCTALRRQRGNMEPIHF 88
Cdd:cd17698     6 KIIRDLQDC-VTELKKEFEETGEPITDDSTTLHKFCAKLEYLLQFDQKEKTTLLGGRKDYWDYFCECLAKVKGLNDGIRF 84

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217327184  89 VRSQDKLKTPLGKGRAFIRFCLARGQLAEALQLCLLNSELTREWYGPRSPLLCPERQEDILDSLYALNGVAFEL 162
Cdd:cd17698    85 VKSLKEVRTSLGKGRAFIRYSLVHQRLADTLQQCVMNGKVTSDWYYPRSVFLNHKYSSDIINSLYDLNEVQFDL 158
RUN_RUFY4_like cd17682
RUN domain found in RUN and FYVE domain-containing protein 4 (RUFY4), FYVE and coiled-coil ...
 21-162 8.93e-45

RUN domain found in RUN and FYVE domain-containing protein 4 (RUFY4), FYVE and coiled-coil domain-containing protein 1 (FYCO1), and similar proteins; The family includes RUFY4 and FYCO1. RUFY4 acts as a positive regulator that enhances autophagy and lysosome tethering in response to Interleukin-4. It is expressed in a cell-specific manner or under specific immunological conditions associated with IL4 expression such as allergic asthma. FYCO1, also called zinc finger FYVE domain-containing protein 7 (ZFYVE7), is a multidomain autophagy adaptor protein that interacts with kinesin motor proteins and with the autophagosomal membrane components microtubule-associated protein 1 light chain 3 (LC3), Rab7, and phosphatidylinositol 3-phosphate (PI3P), to mediate microtubule plus-end-directed autophagosome transport. Both RUFY4 and FYCO1 contain an N-terminal RUN domain and a C-terminal FYVE domain with two coiled-coil domains in-between; this model represents the RUN domain.


Pssm-ID: 439044  Cd Length: 150  Bit Score: 155.08  E-value: 8.93e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327184  21 AILQGYGDGQGPVTDTSAELHRLCGCLELLLQFDQKEQKSFLGPRKDYWDFLCTALRR----QRGNMEPIHFVRSQDKLK 96
Cdd:cd17682     5 CVLDLKSEFGEITDPDNPYLRPFCETLEKILRKGLKEKVSLGGRRKDYWDWLEELLKKlnkiPKSLSDAVKFVKSCKKVK 84

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217327184  97 TPLGKGRAFIRFCLARGQLAEALQLCLLNSELTREWYGPRSPLLCPERQEDILDSLYALNGVAFEL 162
Cdd:cd17682    85 TNQGRGRLFIRYALNKKCLHDPVQQLVKNPKLLSDYYSPDSILGNEILSEILLSLLYQLNEINFDL 150
RUN cd17671
RUN domain; RUN domain, named after RPIP8 (Rap2 interacting protein 8), UNC-14 and NESCA (new ...
 18-162 1.65e-28

RUN domain; RUN domain, named after RPIP8 (Rap2 interacting protein 8), UNC-14 and NESCA (new molecule containing SH3 at the carboxyl-terminus), is a less conserved protein motif that comprises six conserved regions, which in some proteins have considerable insertions between them. The domain core is thought to take up a predominantly alpha fold, with basic amino acids in regions A and D possibly playing a functional role in interactions with Ras GTPases. RUN domains are often found in proteins linked particularly to the functions of GTPases in the Rap and Rab families, suggesting the RUN domain may be involved in Rab-mediated membrane trafficking, possibly as a Rab-binding site. RUN domain-containing proteins could hence play important roles in multiple Ras-like GTPase signalling pathways.


Pssm-ID: 439038  Cd Length: 154  Bit Score: 110.98  E-value: 1.65e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327184  18 AVSAILQGYGDGQG-------PVTDTSAELHRLCGCLELLLQFDQKEqKSFLGPRKDYWDFLCTALRRQRGN--MEPIHF 88
Cdd:cd17671     2 AVKELLESFADNGEaddsaalTLTDDDPVVGRLCAALEAILSHGLKP-KRFGGGKVSFWDFLEALEKLLPAPslKQAIRD 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217327184  89 VRSQDKLKTPLGKGRAFIRFCLARGQLAEALQLCLLNSELTREWYGPRSPLLCPERQEDILDSLYALNGVAFEL 162
Cdd:cd17671    81 INSLSNVKTDDGRGRAWIRLALNEKSLESYLAALLSDQSLLRKYYEPWALLRDPEEAELFLSLLVGLSSLDFNL 154
RUN_RUFY1_like cd17681
RUN domain found in RUN and FYVE domain-containing proteins, RUFY1, RUFY2, RUFY3 and similar ...
 30-162 1.20e-13

RUN domain found in RUN and FYVE domain-containing proteins, RUFY1, RUFY2, RUFY3 and similar proteins; This family includes RUN and FYVE domain-containing protein RUFY1, RUFY2, and RUFY3. RUFY1, also called FYVE-finger protein EIP1, or La-binding protein 1, or Rab4-interacting protein (Rabip4), or Zinc finger FYVE domain-containing protein 12 (ZFY12), a human homolog of mouse Rabip4, an effector of Rab4 GTPase that regulates recycling of endocytosed cargo. RUFY1 is an endosomal protein that functions as a dual effector of Rab4 and Rab14 and is involved in efficient recycling of transferrin (Tfn). It is a downstream effector of Etk, a downstream tyrosine kinase of PI3-kinase that is involved in regulation of vesicle trafficking. RUFY2, also called Rab4-interacting protein related, is a novel embryonic factor that is present in the nucleus at early stages of embryonic development. It may have both endosomal functions in the cytoplasm and nuclear functions. RUFY3, also called Rap2-interacting protein x (RIPx or RPIPx), or single axon-regulated protein (singar), is an N-terminal RUN domain and a C-terminal FYVE domain containing protein predominantly expressed in the brain. It suppresses formation of surplus axons for neuronal polarity. Unlike other RUFY proteins, RUFY3 can associate with the GTP-bound active form of Rab5. RUFY1, RUFY2, and RUFY3 contain an N-terminal RUN domain and a C-terminal FYVE domain with two coiled-coil domains in-between; this model represents the RUN domain.


Pssm-ID: 439043  Cd Length: 155  Bit Score: 68.75  E-value: 1.20e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327184  30 QGPVTDTSAELHRLCGCLELLLQFDQKEQKSFLGPRKDYWDFLCTALRRQRGNMEPIHFVRSQDKLKTPLGKGRAFIRFC 109
Cdd:cd17681    24 GRTLDSDHVPLQQFFVILEHVLRHGLKVKKSFLGPNKSFWPVLEHVEKLVPEANEITASVRDLPGIKTPLGRARAWLRLA 103

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2217327184 110 LARGQLAEALQLCLLNSELTREWYGPRSPLLCPERQEdILDSLYALNGVAFEL 162
Cdd:cd17681   104 LMQKKLADYFRALIENKDLLSEFYEPGALMMSEEAVV-IAGLLVGLNVIDCNL 155
RUN_RUNDC3 cd17684
RUN domain found in RUN domain-containing protein 3 (RUNDC3) and similar proteins; RUNDC3 ...
 31-162 8.32e-11

RUN domain found in RUN domain-containing protein 3 (RUNDC3) and similar proteins; RUNDC3 contains two isoforms, RUNDC3A and RUNDC3B. RUNDC3A, also called Rap2-interacting protein 8 (RPIP8), may act as an effector of Rap2A GTPase in neuronal cells. RUNDC3B, also called Rap2-binding protein 9, or Rap2-interacting protein 9 (RPIP-9), contains a RUN domain in its N-terminal region that mediates interaction with Rap2, an important component of the Mitogen-Activated Protein Kinase (MAPK) cascade, which regulates cellular proliferation and differentiation. It also contains characteristic binding sites for MAPK intermediates. Both RUNDC3A and RUNDC3B contain a RUN domain.


Pssm-ID: 439046  Cd Length: 150  Bit Score: 60.10  E-value: 8.32e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327184  31 GPVTDTSAELHRLCGCLELLLQFDQKEQKSFLG--PRKDYWDFLCTALRRQRGNMepIHFVRSQDKLKTPLGKGRAFIRF 108
Cdd:cd17684    20 ETIDDSSEELINFAAILEQILSHRLKPVKPWYGseEPRTFWDYIRVACKKVPQNC--IASIEQMENIKSPKAKGRAWIRV 97

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2217327184 109 CLARGQLAEALQLCLLNSELTREWYGPRSPLLcperQED---ILDSLYALNGVAFEL 162
Cdd:cd17684    98 ALMEKRLSEYLSTALKQTRLTRNFYQDGAIML----SEDatvLCGMLIGLNAIDFSF 150
RUN pfam02759
RUN domain; This domain is present in several proteins that are linked to the functions of ...
 42-164 9.00e-09

RUN domain; This domain is present in several proteins that are linked to the functions of GTPases in the Rap and Rab families. They could hence play important roles in multiple Ras-like GTPase signalling pathways. The domain is comprises six conserved regions, which in some proteins have considerable insertions between them. The domain core is thought to take up a predominantly alpha fold, with basic amino acids in regions A and D possibly playing a functional role in interactions with Ras GTPases.


Pssm-ID: 460679  Cd Length: 134  Bit Score: 53.82  E-value: 9.00e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327184  42 RLCGCLELLLQ------FDQKEQKSFLGPRKDYWDFL------CTA---LRRQRGNMEPIHfvrsqdKLKTPLGKGRAFI 106
Cdd:pfam02759   1 QLCAALEALLShglkrsSLLILRAAGLLPERSFWALLervgklVPPaeeLLSSVQELEQIH------TPYSPDGRGRAWI 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2217327184 107 RFCLARGQLAEALQLCLLNSELTREWYGPRSPLLCPERQEDILDSLYALNGVAFELDL 164
Cdd:pfam02759  75 RLALNEKLLDQWLKLLLSNKELLSEYYEPWALLADPEFGEILLGLLVGLSALDFNLCL 132
RUN1_DENND5 cd17677
RUN1 domain found in DENN domain-containing protein 5 (DENND5) and similar proteins; DENND5 ...
 29-160 3.39e-08

RUN1 domain found in DENN domain-containing protein 5 (DENND5) and similar proteins; DENND5 has been characterized as Rab6-interacting protein which is composed of an N-terminal DENN (Differentially Expressed in Normal and Neoplastic cells) domain followed by two RUN (RPIP8 [RaP2-interacting protein 8], UNC-14, and NESCA [new molecule containing SH3 at the carboxyl terminus]) domains flanking a PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain. It functions in membrane trafficking at a crossroads between the Golgi and the endosomal system. DENND5 has two isoforms, DENND5A and DENND5B. This model represents the first RUN domain of DENND5.


Pssm-ID: 439039  Cd Length: 183  Bit Score: 53.56  E-value: 3.39e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327184  29 GQGPVTDTSAE----LHRLCGCLELL----LQFDQKeqKSFLgprkdyWDFLCTAL-RRQRGNMEPIHF------VRSQD 93
Cdd:cd17677    37 GHGEVNITGVEentlIASLCDLLERIwshgLQTKQG--KSAL------WSHLLAYQeNEERLKPLPESLlfdmknVQNMK 108

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217327184  94 KLKTPLGKGRAFIRFCLARGQLAEALQLCLLNSELTREWYGPRSPLLCPERQEDILDSLYALNGVAF 160
Cdd:cd17677   109 EIKTDVGYARAWIRLALEKKLLSKHLKTLLSNQDLLRSLYKRYAFLRCEDEREQFLYHLLSLNAVDY 175
RUN_RUNDC3B cd17700
RUN domain found in RUN domain-containing protein 3B (RUNDC3B) and similar proteins; RUN ...
 33-160 4.14e-08

RUN domain found in RUN domain-containing protein 3B (RUNDC3B) and similar proteins; RUN domain-containing protein 3B (RUNDC3B), also called Rap2-binding protein 9, or Rap2-interacting protein 9 (RPIP-9), contains a RUN domain in its N-terminal region that mediates interaction with Rap2, an important component of the Mitogen-Activated Protein Kinase (MAPK) cascade, which regulates cellular proliferation and differentiation. It also contains characteristic binding sites for MAPK intermediates. RUNDC3B contains a RUN domain.


Pssm-ID: 439062  Cd Length: 151  Bit Score: 52.66  E-value: 4.14e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327184  33 VTDTSAELHRLCGCLELLLQFDQKEQKSFLG---PRKdYWDFLCTALRRQRGNMepIHFVRSQDKLKTPLGKGRAFIRFC 109
Cdd:cd17700    22 IDDSSPEFVNFAAILEQILSHRLKGQVTWFGyesPRS-FWDYIRVACSKVPHNC--ICSIENMENVSSSRAKGRAWIRVA 98

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2217327184 110 LARGQLAEALQLCLLNSELTREWYgPRSPLLCPERQEDILDSLYALNGVAF 160
Cdd:cd17700    99 LMEKRLSEYISTALRDFKTTRRFY-EDGAIVLGEEANMLAGMLLGLNAIDF 148
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 402-514 1.28e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.56  E-value: 1.28e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327184 402 ARREEQAEVS-LQDEIKSLRLGLRKAEEQAQRQEQLLREQEGELQALREQLSRCQEERAELQAQLEQKQQEAERRDAMYQ 480
Cdd:COG1196   289 EEYELLAELArLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALL 368

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2217327184 481 EELGGQRDLVQAMKRRVLELIQEKDRLWQRLQHL 514
Cdd:COG1196   369 EAEAELAEAEEELEELAEELLEALRAAAELAAQL 402
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 393-512 2.08e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.79  E-value: 2.08e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327184 393 QVQTEVTLVARREEQAEvsLQDEIKSLRLGLRKAEEQAQRQEQLLREQEGELQALREQLSRCQEERAELQAQ-------- 464
Cdd:COG1196   262 LAELEAELEELRLELEE--LELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEEleeleeel 339

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2217327184 465 --LEQKQQEAERRDAMYQEELGGQRDLVQAMKRRVLELIQEKDRLWQRLQ 512
Cdd:COG1196   340 eeLEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL 389
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
377-538 3.13e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 53.38  E-value: 3.13e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327184  377 VLQGHATKEDSTVENPQVQTEvtLVARREEQAEVSL-QDEIKSLRLGLRKAEEQAQRQEQLLREQEGELQALREQLSRCQ 455
Cdd:COG4913    649 ALQRLAEYSWDEIDVASAERE--IAELEAELERLDAsSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAE 726

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327184  456 EERAELQAQLEQKQQEAERR-----DAMYQEELGGQ--RDLVQAMKRRVLELIQEKDRLWQRLQhlssmapeccvacsKI 528
Cdd:COG4913    727 EELDELQDRLEAAEDLARLElrallEERFAAALGDAveRELRENLEERIDALRARLNRAEEELE--------------RA 792

                          170
                   ....*....|
gi 2217327184  529 FGRFSRRYPC 538
Cdd:COG4913    793 MRAFNREWPA 802
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 404-518 5.99e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 52.63  E-value: 5.99e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327184 404 REEQAEVSLQDEIKSLRLGLRKAEEQAQRQEQLLREQEGELQALREQLSRCQEERAELQAQLEQKQQEAERRDAMYQEEL 483
Cdd:COG1196   299 RLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE 378

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2217327184 484 GGQRDLVQAMKRRVLELIQEKDRLWQRLQHLSSMA 518
Cdd:COG1196   379 EELEELAEELLEALRAAAELAAQLEELEEAEEALL 413
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 404-514 1.33e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.48  E-value: 1.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327184 404 REEQAEVSLQDEIKSLRLGLRKAEEQAQRQEQLLREQEGELQALREQLSRCQEERAELQAQ---LEQKQQEAERRDAMYQ 480
Cdd:COG1196   341 ELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQleeLEEAEEALLERLERLE 420

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2217327184 481 EELGGQRDLVQAMKRRVLELIQEKDRLWQRLQHL 514
Cdd:COG1196   421 EELEELEEALAELEEEEEEEEEALEEAAEEEAEL 454
RUN_RUFY2 cd17695
RUN domain found in RUN and FYVE domain-containing protein 2 (RUFY2) and similar proteins; ...
 47-156 1.60e-06

RUN domain found in RUN and FYVE domain-containing protein 2 (RUFY2) and similar proteins; RUFY2, also called Rab4-interacting protein related, is a novel embryonic factor that contains an N-terminal RUN domain and a C-terminal FYVE domain with two coiled-coil domains in-between. It is present in the nucleus at early stages of embryonic development. It may have both endosomal functions in the cytoplasm and nuclear functions. This model represents the RUN domain of RUFY2.


Pssm-ID: 439057  Cd Length: 156  Bit Score: 48.05  E-value: 1.60e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327184  47 LELLLQFDQKEQKSFLGPRKDYWDFLCTALRRQRGNMEPIHFVRSQDKLKTPLGKGRAFIRFCLARGQLAEALQLCLLNS 126
Cdd:cd17695    41 MEHCLKHGLKVRKSFLSYNKTIWGPLELVEKLCPEAEEIAASVRDLPGLKTPLGRARAWLRLALMQKKLADYLRCLIIRR 120

                          90       100       110
                  ....*....|....*....|....*....|
gi 2217327184 127 ELTREWYgPRSPLLCPERQEDILDSLYALN 156
Cdd:cd17695   121 DLLSEFY-EYHALMMEEEGAVIVGLLVGLN 149
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 403-498 1.83e-06

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 50.15  E-value: 1.83e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327184 403 RREEQAEVSLQDEIKSLRLGLRKAEEQAQRQEQLLREQEGELQALREQLSRCQEERAELQAQLEQKQQE-AERRDAMYQ- 480
Cdd:COG4942    37 AELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEElAELLRALYRl 116

                          90       100
                  ....*....|....*....|....
gi 2217327184 481 ------EELGGQRDLVQAMKRRVL 498
Cdd:COG4942   117 grqpplALLLSPEDFLDAVRRLQY 140
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 393-516 2.33e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 50.71  E-value: 2.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327184 393 QVQTEVTLVARREEQAEVSLQD---EIKSLRLGLRKAEEQAQRQEQLLREQEGELQALREQLSRCQEERAELQAQLEQKQ 469
Cdd:COG1196   243 ELEAELEELEAELEELEAELAEleaELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELE 322

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2217327184 470 QE---AERRDAMYQEELGGQRDLVQAMKRRVLELIQEKDRLWQRLQHLSS 516
Cdd:COG1196   323 EElaeLEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372
RUN1_DENND5B cd17691
RUN1 domain found in DENN domain-containing protein 5B (DENND5B) and similar proteins; DENND5B, ...
 50-160 5.01e-06

RUN1 domain found in DENN domain-containing protein 5B (DENND5B) and similar proteins; DENND5B, also called Rab6-interacting protein 1 (Rab6IP1)-like protein, functions in membrane trafficking at a crossroads between the Golgi and the endosomal system. It is composed of an N-terminal DENN (Differentially Expressed in Normal and Neoplastic cells) domain followed by two RUN (RPIP8 [RaP2-interacting protein 8], UNC-14, and NESCA [new molecule containing SH3 at the carboxyl terminus]) domains flanking a PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain. This model represents the first RUN domain of DENND5B.


Pssm-ID: 439053 [Multi-domain]  Cd Length: 206  Bit Score: 47.36  E-value: 5.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327184  50 LLQFDQKEQKS--------FLGPRKDYWDFLCTALRRQRGNMEPIHFVRSQDKLKTPLGKGRAFIRFCLARGQLAEALQL 121
Cdd:cd17691    80 LLHFQEREEKQehvaespvANGLERRKSETGVNLPTLRVSLIQDMRHIQNMSEIKTDVGRARAWIRLSLEKKLLSQHLKQ 159

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2217327184 122 CLLNSELTREWYGPRSPLLCPERQEDILDSLYALNGVAF 160
Cdd:cd17691   160 LLSNQALTKKLYKRYAFLRCEEEKEQFLYHLLSLNAVDY 198
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 398-517 5.87e-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: 49.28  E-value: 5.87e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327184  398 VTLVARREEQAEVsLQDEIKSLRLGLRKAEEQAQRQEQLLREQEGELQALREQLSRCQEERAELQAQLE---QKQQEAER 474
Cdd:TIGR02168  294 ANEISRLEQQKQI-LRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEeleAELEELES 372

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 2217327184  475 RDAMYQEELGGQRDLVQAMKRRVLELIQEKDRLWQRLQHLSSM 517
Cdd:TIGR02168  373 RLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDR 415
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 404-514 6.69e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.16  E-value: 6.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327184 404 REEQAEVSLQ-DEIKSLRLGLRKAEEQAQRQEQLLREQEGELQALREQLSRCQEERAELQAQLEQKQQ---EAERRDAMY 479
Cdd:COG1196   221 ELKELEAELLlLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAeeyELLAELARL 300

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2217327184 480 QEELGGQRDLVQAMKRRVLELIQEKDRLWQRLQHL 514
Cdd:COG1196   301 EQDIARLEERRRELEERLEELEEELAELEEELEEL 335
RUN_RUFY3 cd17696
RUN domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar proteins; ...
 38-156 7.99e-06

RUN domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar proteins; RUFY3, also called Rap2-interacting protein x (RIPx or RPIPx), or single axon-regulated protein (singar), is an N-terminal RUN domain and a C-terminal FYVE domain containing protein predominantly expressed in the brain. It suppresses formation of surplus axons for neuronal polarity. Unlike other RUFY proteins, RUFY3 can associate with the GTP-bound active form of Rab5. This model represents the RUN domain of RUFY3.


Pssm-ID: 439058  Cd Length: 156  Bit Score: 46.14  E-value: 7.99e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327184  38 AELHRLCGCLELLLQFDQKEQKSFLGPRKDYWDFLCTALRRQRGNMEPIHFVRSQDKLKTPLGKGRAFIRFCLARGQLAE 117
Cdd:cd17696    32 APLQQFFVVMEHCLKHGLKAKKTFLGQNKSFWGPLELVEKLVPEAAEITASVKDLPGLKTPVGRGRAWLRLALMQKKLSE 111

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2217327184 118 ALQLCLLNSELTREWYGPRSpLLCPERQEDILDSLYALN 156
Cdd:cd17696   112 YMKALINRKDLLSEFYEPNA-LMMEEEGAIIAGLLVGLN 149
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 395-514 1.13e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.39  E-value: 1.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327184 395 QTEVTLVARREEQAEVSLQDEIKSLRLGLRKAEEQAQRQEQLLREQEGELQALREQLSRcQEERAELQAQLEQKQQEAER 474
Cdd:COG1196   350 EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEA-EEALLERLERLEEELEELEE 428

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2217327184 475 RDAMYQEELGGQRDLVQAMKRRVLELIQEKDRLWQRLQHL 514
Cdd:COG1196   429 ALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL 468
RUN smart00593
domain involved in Ras-like GTPase signaling;
102-164 1.14e-05

domain involved in Ras-like GTPase signaling;


Pssm-ID: 214736 [Multi-domain]  Cd Length: 64  Bit Score: 42.99  E-value: 1.14e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217327184  102 GRAFIRFCLARGQLAEALQLCLLNSELTREWYGPRSPLLCPERQEDILDSLYALNGVAFELDL 164
Cdd:smart00593   1 FRAWIRLALNEKLLSSWLNLLLSDEELLSKYYEPWAFLRDPEEGEQLLGLLVGLSALDFNLPV 63
HlpA COG2825
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ...
 427-503 1.20e-05

Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442073 [Multi-domain]  Cd Length: 171  Bit Score: 45.60  E-value: 1.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327184 427 EEQAQRQEQLLREQEGELQALREQLSR-----CQEERAELQAQLEQKQQEAERRDAMYQEELGG-QRDLVQAMKRRVLEL 500
Cdd:COG2825    49 EKEFKKRQAELQKLEKELQALQEKLQKeaatlSEEERQKKERELQKKQQELQRKQQEAQQDLQKrQQELLQPILEKIQKA 128


                  ...
gi 2217327184 501 IQE 503
Cdd:COG2825   129 IKE 131
RUN_PLEKHM2 cd17680
RUN domain found in pleckstrin homology domain-containing family M member 2 (PLEKHM2) and ...
 33-162 1.28e-05

RUN domain found in pleckstrin homology domain-containing family M member 2 (PLEKHM2) and similar proteins; PLEKHM2, also called PH domain-containing family M member 2, or Salmonella-induced filaments A (SifA) and Kinesin-Interacting Protein (SKIP), is the lysosome, melanosome and lytic granule cargo adaptor that controls lysosome positioning using a composite kinesin-1 heavy and light chain-binding domain. In addition to kinesin-1, it also interacts with several Rabs to affect endosomal trafficking. This model represents the RUN domain of PLEKHM2.


Pssm-ID: 439042  Cd Length: 145  Bit Score: 45.31  E-value: 1.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327184  33 VTDTSAELHRLCGCLELLLQFdqkeqkSFLGPRKDYWDFLCTALRRQRgnmepIHFVRSQDKLKTPLGKGRAFIRFCLAR 112
Cdd:cd17680    27 ITNENRELQRLCEALDHALLH------GLRRGNRGYWPFVKEFTHKET-----IKQIENLPNVTTDLGRGRAWLYLALNE 95

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2217327184 113 GQLAEALQLCLLNSELTREWYGPRSPLLCPERQEDILDSLYALNGVAFEL 162
Cdd:cd17680    96 GSLESYLRSFLENRKLVKKFYHKHALLRDSQRLELLLTLLSGLEFVQFDL 145
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 395-507 1.54e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.01  E-value: 1.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327184 395 QTEVTLVARREEQAEVSLQDEIKSLRLGLRKAEEQAQRQEQLLREQEGELQALREQLSRCQEERAELQAQLEQKQQEAER 474
Cdd:COG1196   318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAE 397

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2217327184 475 RDAMYQEELGGQRDLVQAMKRRVLELIQEKDRL 507
Cdd:COG1196   398 LAAQLEELEEAEEALLERLERLEEELEELEEAL 430
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
399-512 2.13e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.60  E-value: 2.13e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327184  399 TLVARREEQAEVSLQDEIKSLRLGLRKAEEQAQRQEQLLREQEGELQALREQ--------LSRCQEERAELQAQLEQKQQ 470
Cdd:COG4913    280 ALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQirgnggdrLEQLEREIERLERELEERER 359

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 2217327184  471 EAERRD---AMYQEELGGQRDLVQAMKRRVLELIQEKDRLWQRLQ 512
Cdd:COG4913    360 RRARLEallAALGLPLPASAEEFAALRAEAAALLEALEEELEALE 404
hsdR PRK11448
type I restriction enzyme EcoKI subunit R; Provisional
 406-506 2.64e-05

type I restriction enzyme EcoKI subunit R; Provisional


Pssm-ID: 236912 [Multi-domain]  Cd Length: 1123  Bit Score: 47.25  E-value: 2.64e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327184  406 EQAEVSLQDEIKSLRLGLRKAEEQAQRQEQLLREQEGELQALREQLSRCQEERAELQAQLEQKQQEAERRDAMYQEELGG 485
Cdd:PRK11448   141 ENLLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAETSQERKQKRKE 220

                           90       100
                   ....*....|....*....|.
gi 2217327184  486 QRDlvQAMKRrvLELIQEKDR 506
Cdd:PRK11448   221 ITD--QAAKR--LELSEEETR 237
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 393-517 2.89e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 46.97  E-value: 2.89e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327184  393 QVQTEVTLVARREEQAEvSLQDEIKSLRlglRKAEEQAQRQEQLLREQEGELQALRE-QLSRCQEERAELQAQLEQKQQE 471
Cdd:TIGR02168  380 QLETLRSKVAQLELQIA-SLNNEIERLE---ARLERLEDRRERLQQEIEELLKKLEEaELKELQAELEELEEELEELQEE 455

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 2217327184  472 AERRdamyQEELGGQRDLVQAMKRRVLELIQEKDRLWQRLQHLSSM 517
Cdd:TIGR02168  456 LERL----EEALEELREELEEAEQALDAAERELAQLQARLDSLERL 497
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
393-510 2.98e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.83  E-value: 2.98e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327184  393 QVQTEVTLVARREEQAEVSLQ----DEIKSLRLGLRKAEEQAQRQEQLLREQEGELQALREQLSRCQEERAELQAQLEQK 468
Cdd:COG4913    313 RLEARLDALREELDELEAQIRgnggDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAAL 392

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 2217327184  469 QQEAERRDAMYQEELGGQRDLVQAMKRRVLELIQEKDRLWQR 510
Cdd:COG4913    393 LEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 402-512 3.42e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.85  E-value: 3.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327184 402 ARREEQAEVSLQDEIKSLRlglRKAEEQAQRQEQLLREQEGELQALREQLSRCQEERAEL---QAQLEQKQQEAERRDAM 478
Cdd:COG1196   388 LLEALRAAAELAAQLEELE---EAEEALLERLERLEEELEELEEALAELEEEEEEEEEALeeaAEEEAELEEEEEALLEL 464

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2217327184 479 YQEELGGQRDLVQAMKRRVLELIQEKDRLWQRLQ 512
Cdd:COG1196   465 LAELLEEAALLEAALAELLEELAEAAARLLLLLE 498
RUN_RUNDC3A cd17699
RUN domain found in RUN domain-containing protein 3A (RUNDC3A) and similar proteins; RUN ...
 18-133 3.64e-05

RUN domain found in RUN domain-containing protein 3A (RUNDC3A) and similar proteins; RUN domain-containing protein 3A (RUNDC3A), also called Rap2-interacting protein 8 (RPIP8), may act as an effector of Rap2A GTPase in neuronal cells. It contains a RUN domain.


Pssm-ID: 439061  Cd Length: 151  Bit Score: 43.86  E-value: 3.64e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327184  18 AVSAILQGYGdgQGPVTDTSAELHRLCGCLELLLQFDQKEQKSFLGP--RKDYWDFLCTALRRQRGNMepIHFVRSQDKL 95
Cdd:cd17699     9 SVKTLLEKYT--AEPIDDSSEEFVNFAAILEQILSHRFKGPVSWFSSdgQRGFWDYIRLACSKVPNNC--ISSIENMENI 84

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2217327184  96 KTPLGKGRAFIRFCLARGQLAEALQLCLLNSELTREWY 133
Cdd:cd17699    85 STSRAKGRAWIRVALMEKRLSEYIATALRDTRTTRRFY 122
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 393-499 3.75e-05

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 46.65  E-value: 3.75e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327184  393 QVQTEVTLVARR----EEQAEVSLQDEIKSLRLGLRKAEEqaqRQEQLLREQEGELQALREQLSRCQEERAELQAQLEQK 468
Cdd:pfam15921  228 ELDTEISYLKGRifpvEDQLEALKSESQNKIELLLQQHQD---RIEQLISEHEVEITGLTEKASSARSQANSIQSQLEII 304

                           90       100       110
                   ....*....|....*....|....*....|.
gi 2217327184  469 QQEAERRDAMYQEELGGQRDLVQAMKRRVLE 499
Cdd:pfam15921  305 QEQARNQNSMYMRQLSDLESTVSQLRSELRE 335
Lebercilin pfam15619
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ...
 411-512 3.77e-05

Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.


Pssm-ID: 464776 [Multi-domain]  Cd Length: 193  Bit Score: 44.51  E-value: 3.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327184 411 SLQDEIKSLRLGLRKAEEQAQRQEQLLREQEGELQALREQLSRCQE--------ERAELQAQLEQKQQEAERRDAM---- 478
Cdd:pfam15619  64 RHNEEVRVLRERLRRLQEKERDLERKLKEKEAELLRLRDQLKRLEKlsedknlaEREELQKKLEQLEAKLEDKDEKiqdl 143

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2217327184 479 ----------YQEELGGQRDLVQAMKRRVLELIQEKDRLWQRLQ 512
Cdd:pfam15619 144 erklelenksFRRQLAAEKKKHKEAQEEVKILQEEIERLQQKLK 187
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 393-514 4.12e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.47  E-value: 4.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327184 393 QVQTEVTLVARREEQAEVS-LQDEIKSLRLGLRKAEEQAQRQEQLLREQEGELQALREQLSRCQEERAELQ---AQLEQK 468
Cdd:COG1196   224 ELEAELLLLKLRELEAELEeLEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLaelARLEQD 303

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2217327184 469 -------QQEAERRDAMYQEELGGQRDLVQAMKRRVLELIQEKDRLWQRLQHL 514
Cdd:COG1196   304 iarleerRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA 356
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 424-507 4.39e-05

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 46.36  E-value: 4.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327184 424 RKAEEQAQRQEQLLREQEGELQALREQLSRCQEERAELQAQLEQKQQEA-----ERRDAMYQEELGGQRDLVQAMKRRvl 498
Cdd:PRK00409  530 RELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAikeakKEADEIIKELRQLQKGGYASVKAH-- 607


                  ....*....
gi 2217327184 499 ELIQEKDRL 507
Cdd:PRK00409  608 ELIEARKRL 616
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 402-517 4.57e-05

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


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 46.27  E-value: 4.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327184 402 ARREEQAEVSLQDEIKSLRLGLRKAEEQAQRQEQLLREQEGELQALREQL----SRCQE---ERAELQAQL------EQK 468
Cdd:pfam05557  92 LNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLdllkAKASEaeqLRQNLEKQQsslaeaEQR 171

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2217327184 469 QQEAERRDAMYQEElggqRDLVQAMKRRVL---ELIQEKDRLWQRLQHLSSM 517
Cdd:pfam05557 172 IKELEFEIQSQEQD----SEIVKNSKSELAripELEKELERLREHNKHLNEN 219
mukB PRK04863
chromosome partition protein MukB;
403-514 4.96e-05

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 46.49  E-value: 4.96e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327184  403 RREEQAEVSLQDEIKSLRLGLRKAEEQaqrqEQLLREQEGELQALREQLSRCQEERAELQAQLEQKQQE----------- 471
Cdd:PRK04863   530 RQQQRAERLLAEFCKRLGKNLDDEDEL----EQLQEELEARLESLSESVSEARERRMALRQQLEQLQARiqrlaarapaw 605

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2217327184  472 ------AERRDAMYQEELGGQRDLVQAMK---RRVLELIQEKDRLWQRLQHL 514
Cdd:PRK04863   606 laaqdaLARLREQSGEEFEDSQDVTEYMQqllERERELTVERDELAARKQAL 657
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 402-516 5.01e-05

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 46.48  E-value: 5.01e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327184  402 ARREEQAEVSLQDEIKSLRLGLRKAEEQaqrqEQLLREQEGELQALREQLSRCQEERAELQAQLEQ-------------- 467
Cdd:COG3096    528 LRQQQNAERLLEEFCQRIGQQLDAAEEL----EELLAELEAQLEELEEQAAEAVEQRSELRQQLEQlrarikelaarapa 603

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2217327184  468 ---KQQEAERRDAMYQEELGGQRDLVQAMK---RRVLELIQEKDRLWQRLQHLSS 516
Cdd:COG3096    604 wlaAQDALERLREQSGEALADSQEVTAAMQqllEREREATVERDELAARKQALES 658
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
401-514 5.12e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.06  E-value: 5.12e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327184  401 VARREEQAE-----VSLQDEIKSLRLGLRKAEE-----QAQRQEQLLREQEGELQALREQLSRCQEERAELQAQLEQKQQ 470
Cdd:COG4913    244 LEDAREQIEllepiRELAERYAAARERLAELEYlraalRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALRE 323

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 2217327184  471 EAERRDAMYQEELGGQRDLVQAMKRRVLELIQEKDRLWQRLQHL 514
Cdd:COG4913    324 ELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEAL 367
MIC19_MIC25 pfam05300
MICOS complex subunit MIC19/MIC25; MIC19 (also known as ChChd3) and MIC25 (also known as ...
 424-484 6.63e-05

MICOS complex subunit MIC19/MIC25; MIC19 (also known as ChChd3) and MIC25 (also known as ChChd6) are components of the MICOS complex, a large protein complex of the mitochondrial inner membrane that plays crucial roles in the maintenance of crista junctions, inner membrane architecture, and formation of contact sites to the outer membrane. MIC19 plays an important role in the maintenance of the MICOS complex stability and the mitochondrial cristae morphology.


Pssm-ID: 461615 [Multi-domain]  Cd Length: 173  Bit Score: 43.53  E-value: 6.63e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217327184 424 RKAEEQAQRQEQLLREQEGELQALREQLSRC--------QEER---AELQAQLEQKQQEAERRDAMYQEELG 484
Cdd:pfam05300  74 RLEQEQAKVQEELARLAEREREAAQESLTRAilrerastEDERlkaQQLAKQLEEKEAELKKQDAFYKEQLA 145
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 393-512 6.72e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.70  E-value: 6.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327184 393 QVQTEVTLVARREEQAEVSLQDEIKSLRlglRKAEEQAQRQEQL------LREQEGELQALREQLSRCQEERAELQAQLE 466
Cdd:COG1196   299 RLEQDIARLEERRRELEERLEELEEELA---ELEEELEELEEELeeleeeLEEAEEELEEAEAELAEAEEALLEAEAELA 375

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2217327184 467 QKQQEAERRDAMYQEELGGQRDLVQAMKRRVLELIQEKDRLWQRLQ 512
Cdd:COG1196   376 EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEE 421
RUN_PLEKHM1 cd17679
RUN domain found in pleckstrin homology domain-containing family M member 1 (PLEKHM1) and ...
 16-164 8.49e-05

RUN domain found in pleckstrin homology domain-containing family M member 1 (PLEKHM1) and similar proteins; PLEKHM1, also called PH domain-containing family M member 1, or 162 kDa adapter protein (AP162), may act as a multivalent adapter protein that regulates Rab7-dependent and HOPS complex-dependent fusion events in the endolysosomal system and couples autophagic and the endocytic trafficking pathways. This model represents the RUN domain of PLEKHM1.


Pssm-ID: 439041 [Multi-domain]  Cd Length: 171  Bit Score: 43.35  E-value: 8.49e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327184  16 AAAVSAILQGYGDGQGPVTDTSAELHRLCGCLE-LLLQ-----FDQKEQKSFLG-----PRKDYWDFLCTALRRQrgnme 84
Cdd:cd17679     9 SSSVKELQLEYVSSDEVVTSSDDGANTLCCVLEaIFLHglkdkFISKVSSVFSGdvdklPEPNFWPLLLKFSHRD----- 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327184  85 pihfVRSQ-DKL---KTPLGKGRAFIRFCLARGQLAEALQLCLLNSELTREWYGPRSPLLCPERQEDILDSLYALNGVAF 160
Cdd:cd17679    84 ----VIDQiEHLsqiTTDVGRCRAWIRLALNDGLLESYLEAILKDKSALKSYYNPSAFLRDPEQLDILKSLLQGLESFQF 159


                  ....
gi 2217327184 161 ELDL 164
Cdd:cd17679   160 ELPY 163
OmpH pfam03938
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 427-503 8.51e-05

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 461098 [Multi-domain]  Cd Length: 140  Bit Score: 42.56  E-value: 8.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327184 427 EEQAQRQEQLLREQEGELQALREQL----SRCQEERAELQAQLEQKQQEAERRDAMYQEELGG-QRDLVQAMKRRVLELI 501
Cdd:pfam03938  25 EKKFKKRQAELEAKQKELQKLYEELqkdgALLEEEREEKEQELQKKEQELQQLQQKAQQELQKkQQELLQPIQDKINKAI 104


                  ..
gi 2217327184 502 QE 503
Cdd:pfam03938 105 KE 106
PRK12704 PRK12704
phosphodiesterase; Provisional
 412-483 1.25e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 44.77  E-value: 1.25e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217327184 412 LQDEIKSLRLGLRKAEEQAQRQEQLLREQEGELQALREQLSRCQEERAELQAQLEQKQQEAERRDAMYQEEL 483
Cdd:PRK12704   73 FEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQEL 144
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 372-516 1.29e-04

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: 45.06  E-value: 1.29e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327184  372 LGEPWVLQGHATKEDSTVENPQVQTEVTLVARREEQAEVSLQdeikslrlglrKAEEQAQRQEQLLREQEGELQALREQL 451
Cdd:TIGR02169  284 LGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLA-----------KLEAEIDKLLAEIEELEREIEEERKRR 352

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217327184  452 SRCQEERAELQAQLEQKQQEAERRDAMYQE---ELGGQRDLVQAMKRRVLELIQEKDRLWQRLQHLSS 516
Cdd:TIGR02169  353 DKLTEEYAELKEELEDLRAELEEVDKEFAEtrdELKDYREKLEKLKREINELKRELDRLQEELQRLSE 420
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
384-507 1.32e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 45.03  E-value: 1.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327184 384 KEDSTVENPQVQTEVTLVARREEQAE--VSLQDEIKSLRlglrkaeEQAQRQEQLLREQEGELQALREQLSRCQEERAEL 461
Cdd:PRK02224  477 VEELEAELEDLEEEVEEVEERLERAEdlVEAEDRIERLE-------ERREDLEELIAERRETIEEKRERAEELRERAAEL 549

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2217327184 462 QAQLEQKQQEAERRdamyQEELGGQRDLVQAMKRRVLELIQEKDRL 507
Cdd:PRK02224  550 EAEAEEKREAAAEA----EEEAEEAREEVAELNSKLAELKERIESL 591
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
419-512 1.38e-04

Multidrug resistance efflux pump EmrA [Defense mechanisms];


Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 44.27  E-value: 1.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327184 419 LRLGLRKAEEQAQRQEQLLREQEGELQAlREQLSRCQEERAELQAQLEQKQQEAERRDAMYQEELGGQRDLVQAmKRRVL 498
Cdd:COG1566    81 LQAALAQAEAQLAAAEAQLARLEAELGA-EAEIAAAEAQLAAAQAQLDLAQRELERYQALYKKGAVSQQELDEA-RAALD 158

                          90
                  ....*....|....
gi 2217327184 499 ELIQEKDRLWQRLQ 512
Cdd:COG1566   159 AAQAQLEAAQAQLA 172
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 385-515 1.60e-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: 44.66  E-value: 1.60e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327184  385 EDSTVENPQVQTEVTLVARREEQAE-VSLQDEIKSLRLGLRKAEEQAQRQEQLLREQEGELQALREQLSRCQEERAELQA 463
Cdd:TIGR02168  752 LSKELTELEAEIEELEERLEEAEEElAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLER 831

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2217327184  464 QLEQKQQEAERRdamyQEELGGQRDLVQAMKRRVLELIQEKDRLWQRLQHLS 515
Cdd:TIGR02168  832 RIAATERRLEDL----EEQIEELSEDIESLAAEIEELEELIEELESELEALL 879
PRK12704 PRK12704
phosphodiesterase; Provisional
 402-520 1.74e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 44.38  E-value: 1.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327184 402 ARRE-----EQAEVSLQDEIKSLRlglRKAEEQAQRQEQLLREQEGELQALREQLSRCQEERAELQAQLEQKQQEAERRd 476
Cdd:PRK12704   47 AKKEaeaikKEALLEAKEEIHKLR---NEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQK- 122

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2217327184 477 amyQEELggqrdlvQAMKRRVLELIQEKDrlwQRLQHLSSMAPE 520
Cdd:PRK12704  123 ---QQEL-------EKKEEELEELIEEQL---QELERISGLTAE 153
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 400-496 1.95e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 43.98  E-value: 1.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327184 400 LVARREEQAEvSLQDEIKSLRLGLRKAEEQAQRQEQLLREQEGELQALREQlsrcQEERAELQAQLEQKQQEAERRDAMY 479
Cdd:COG4942   144 LAPARREQAE-ELRADLAELAALRAELEAERAELEALLAELEEERAALEAL----KAERQKLLARLEKELAELAAELAEL 218

                          90
                  ....*....|....*..
gi 2217327184 480 QEELGGQRDLVQAMKRR 496
Cdd:COG4942   219 QQEAEELEALIARLEAE 235
PRK12705 PRK12705
hypothetical protein; Provisional
 403-520 1.96e-04

hypothetical protein; Provisional


Pssm-ID: 237178 [Multi-domain]  Cd Length: 508  Bit Score: 43.93  E-value: 1.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327184 403 RREEQAEVSLQDEIKSLRLGLRKAeeQAQRQEQLLREQEGELQALREQLSRCQEERAELQAQLEQKQQEAERRDAMYQEE 482
Cdd:PRK12705   30 RLAKEAERILQEAQKEAEEKLEAA--LLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKLDNLENQL 107

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2217327184 483 LGGQRdlvqAMKRRVLELIQEKDRLWQRLQHLSSMAPE 520
Cdd:PRK12705  108 EEREK----ALSARELELEELEKQLDNELYRVAGLTPE 141
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 416-503 2.12e-04

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 44.40  E-value: 2.12e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327184  416 IKSLRLGLRKAEEQAQRQEQLLREQEGELQALREQLSRCQEERAELQAQLEQKQQEAERRDAMYQEElGGQRDLVQAMKR 495
Cdd:pfam01576  189 ISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEE-TAQKNNALKKIR 267


                   ....*...
gi 2217327184  496 RVLELIQE 503
Cdd:pfam01576  268 ELEAQISE 275
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 404-514 2.25e-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: 44.28  E-value: 2.25e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327184  404 REEQAEVS-LQDEIKSLRLGLRK-------AEEQAQRQEQLLREQEGELQALREQLSRCQEERAELQAQLEQKQQE---A 472
Cdd:TIGR02168  806 DELRAELTlLNEEAANLRERLESlerriaaTERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNErasL 885

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 2217327184  473 ERRDAMYQEELGGQRDLVQAMKRRVLELIQEKDRLWQRLQHL 514
Cdd:TIGR02168  886 EEALALLRSELEELSEELRELESKRSELRRELEELREKLAQL 927
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 405-515 2.29e-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: 44.28  E-value: 2.29e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327184  405 EEQAEVS-----LQDEIKSLRLGLRKAEEQAQRQEqlLREQEGELQALREQLSRCQEERAELQAQLEQ---KQQEAERRD 476
Cdd:TIGR02168  206 ERQAEKAerykeLKAELRELELALLVLRLEELREE--LEELQEELKEAEEELEELTAELQELEEKLEElrlEVSELEEEI 283

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 2217327184  477 AMYQEELGGQRDLVQAMKRRVLELIQEKDRLWQRLQHLS 515
Cdd:TIGR02168  284 EELQKELYALANEISRLEQQKQILRERLANLERQLEELE 322
Mitofilin pfam09731
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ...
 407-504 2.39e-04

Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.


Pssm-ID: 430783 [Multi-domain]  Cd Length: 618  Bit Score: 43.98  E-value: 2.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327184 407 QAEVSLQDEIKSLRLGLRK-AEEQAQRQE--------QLLREQEGELQALREQLsrcqeeRAELQAQLEQKQQEAERRda 477
Cdd:pfam09731 309 REEKHIERALEKQKEELDKlAEELSARLEevraadeaQLRLEFEREREEIRESY------EEKLRTELERQAEAHEEH-- 380

                          90       100
                  ....*....|....*....|....*..
gi 2217327184 478 mYQEELGGQRdlvQAMKRRVLELIQEK 504
Cdd:pfam09731 381 -LKDVLVEQE---IELQREFLQDIKEK 403
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
404-516 2.40e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 43.35  E-value: 2.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327184 404 REEQAEVSLQDEIKSLRLGLRKAEEQAQRQEQLLREQEGELQALREQLSRCQEERAELQAQLEQKQ---QEAERRDAMYQ 480
Cdd:COG4372    21 KTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNeqlQAAQAELAQAQ 100

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2217327184 481 EELGGQRDLVQAMKRRVLELIQEKDRLWQRLQHLSS 516
Cdd:COG4372   101 EELESLQEEAEELQEELEELQKERQDLEQQRKQLEA 136
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 395-486 2.42e-04

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


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 43.92  E-value: 2.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327184 395 QTEVTLVARREEQAEVS------LQDEIKSLRLGLRKAEEQAQRQEQLLREqegeLQALREQLSRCQEERAELQAQLEQK 468
Cdd:COG0542   422 QLEIEKEALKKEQDEASferlaeLRDELAELEEELEALKARWEAEKELIEE----IQELKEELEQRYGKIPELEKELAEL 497

                          90
                  ....*....|....*...
gi 2217327184 469 QQEAERRDAMYQEELGGQ 486
Cdd:COG0542   498 EEELAELAPLLREEVTEE 515
RUN_RUFY1 cd17694
RUN domain found in RUN and FYVE domain-containing protein 1 (RUFY1) and similar proteins; ...
 47-156 2.84e-04

RUN domain found in RUN and FYVE domain-containing protein 1 (RUFY1) and similar proteins; RUFY1, also called FYVE-finger protein EIP1, or La-binding protein 1, or Rab4-interacting protein (Rabip4), or Zinc finger FYVE domain-containing protein 12 (ZFY12), a human homolog of mouse Rabip4, an effector of Rab4 GTPase that regulates recycling of endocytosed cargo. RUFY1 is an endosomal protein that functions as a dual effector of Rab4 and Rab14 and is involved in efficient recycling of transferrin (Tfn). It is a downstream effector of Etk, a downstream tyrosine kinase of PI3-kinase that is involved in regulation of vesicle trafficking. RUFY1 contains an N-terminal RUN domain and a C-terminal FYVE domain with two coiled-coil domains in-between; this model represents the RUN domain.


Pssm-ID: 439056  Cd Length: 156  Bit Score: 41.43  E-value: 2.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327184  47 LELLLQFDQKEQKSFLGPRKDYWDFLCTALRRQRGNMEPIHFVRSQDKLKTPLGKGRAFIRFCLARGQLAEALQLCLLNS 126
Cdd:cd17694    41 LEHCLKHGLKVKKSFIGQNKSFFGPLELVEKLCPEASDIATSARNLPELKTAVGRGRAWLHLALMQKKLADYLKVLIDRK 120

                          90       100       110
                  ....*....|....*....|....*....|
gi 2217327184 127 ELTREWYGPRSpLLCPERQEDILDSLYALN 156
Cdd:cd17694   121 DLLSEFYEPGA-LMMEEEGAVIVGLLVGLN 149
RUN1_DENND5A cd17690
RUN1 domain found in DENN domain-containing protein 5A (DENND5A) and similar proteins; DENND5A, ...
 50-160 3.75e-04

RUN1 domain found in DENN domain-containing protein 5A (DENND5A) and similar proteins; DENND5A, also called Rab6-interacting protein 1 (Rab6IP1), is present predominantly in developing neuronal tissue, and functions in membrane trafficking at a crossroads between the Golgi and the endosomal system. It is composed of an N-terminal DENN (Differentially Expressed in Normal and Neoplastic cells) domain followed by two RUN (RPIP8 [RaP2-interacting protein 8], UNC-14, and NESCA [new molecule containing SH3 at the carboxyl terminus]) domains flanking a PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain. This model represents the first RUN domain of DENND5A.


Pssm-ID: 439052 [Multi-domain]  Cd Length: 209  Bit Score: 41.92  E-value: 3.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327184  50 LLQFDQKEQKSFLGPRKDYWDFLCTALRRQRGN---MEPIHFVRSQD--------KLKTPLGKGRAFIRFCLARGQLAEA 118
Cdd:cd17690    80 LLHYQENRERKTTSSGLSTSGIILDSERRKSDAslaMPPLKISLIQDmrhiqnigEIKTDVGKARAWVRLSMEKKLLSRH 159

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2217327184 119 LQLCLLNSELTREWYGPRSPLLCPERQEDILDSLYALNGVAF 160
Cdd:cd17690   160 LKQLLSDHELTKKLYKRYAFLRCDDEKEQFLYHLLSFNAVDY 201
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 423-521 4.03e-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: 4.03e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327184  423 LRKAEEQAQRQEQLLREQEGELQALREQLSRCQEERAELQAQLEQKQQEAERRDAMYQEELGGQRDLVQAMKR---RVLE 499
Cdd:TIGR02168  679 IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQlskELTE 758

                           90       100
                   ....*....|....*....|..
gi 2217327184  500 LIQEKDRLWQRLQHLSSMAPEC 521
Cdd:TIGR02168  759 LEAEIEELEERLEEAEEELAEA 780
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
388-470 4.16e-04

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 43.08  E-value: 4.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327184 388 TVENPQVQTevtlvARRE-EQAEVSLQDEIKSLRLGLRKAEEQAQRQEQLLREQEGELQALREQLSRCQEERAELQAQLE 466
Cdd:COG3206   287 TPNHPDVIA-----LRAQiAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVE 361


                  ....
gi 2217327184 467 QKQQ 470
Cdd:COG3206   362 VARE 365
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 407-483 4.27e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 42.89  E-value: 4.27e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217327184 407 QAEVSLQDEIKSLRLGLRKAEEQAQRQEQLLREQEGELQALREQLSRCQEERAELQAQLEQKQQEAERRDAMYQEEL 483
Cdd:COG3883   129 DADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAEL 205
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 412-515 4.36e-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: 43.12  E-value: 4.36e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327184  412 LQDEIKSLRLGLRKAEEQAQRQEQL------------------LREQEGELQALREQLSRCQEERAELQAQLEQKQQEAE 473
Cdd:TIGR02168  191 LEDILNELERQLKSLERQAEKAERYkelkaelrelelallvlrLEELREELEELQEELKEAEEELEELTAELQELEEKLE 270

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 2217327184  474 R-RDAMYQEElggqrDLVQAMKRRVLELIQEKDRLWQRLQHLS 515
Cdd:TIGR02168  271 ElRLEVSELE-----EEIEELQKELYALANEISRLEQQKQILR 308
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
393-503 4.92e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.58  E-value: 4.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327184 393 QVQTEVTLVARREEQAEvSLQDEIKSLRLGLRKAEEQAQRQEQLLREQEGELQALREQLSRCQEERAELQAQLEQKQQEA 472
Cdd:COG4372    32 QLRKALFELDKLQEELE-QLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEA 110

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2217327184 473 ERRDAmYQEELGGQRDLVQAMKRRVLELIQE 503
Cdd:COG4372   111 EELQE-ELEELQKERQDLEQQRKQLEAQIAE 140
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 425-503 4.97e-04

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 214922 [Multi-domain]  Cd Length: 140  Bit Score: 40.26  E-value: 4.97e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327184  425 KAEEQAQRQEQLLREQEGELQALREQLSR-----CQEERAELQAQLEQKQQEAERRDAMYQEEL-GGQRDLVQAMKRRVL 498
Cdd:smart00935  22 QLEKEFKKRQAELEKLEKELQKLKEKLQKdaatlSEAAREKKEKELQKKVQEFQRKQQKLQQDLqKRQQEELQKILDKIN 101


                   ....*
gi 2217327184  499 ELIQE 503
Cdd:smart00935 102 KAIKE 106
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
406-514 5.05e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.83  E-value: 5.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327184 406 EQAEVSLQDEIKSLRLGLRKAEEQAQRQEQLLREQ--EGELQALREQLSRCQEERAELQaQLEQKQQEAERRDAMYQEEL 483
Cdd:COG4717   101 EEELEELEAELEELREELEKLEKLLQLLPLYQELEalEAELAELPERLEELEERLEELR-ELEEELEELEAELAELQEEL 179

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2217327184 484 GGQRDLV-QAMKRRVLELIQEKDRLWQRLQHL 514
Cdd:COG4717   180 EELLEQLsLATEEELQDLAEELEELQQRLAEL 211
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 393-512 5.49e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.00  E-value: 5.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327184 393 QVQTEVTLVARREEQAEVSLQDEIKSLRLGLRKAEEQAQRQEQLLREQEgELQALREQLSRCQEERAELQAQLEQKQQEA 472
Cdd:COG1196   408 AEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEE-EEEALLELLAELLEEAALLEAALAELLEEL 486

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2217327184 473 ER---RDAMYQEELGGQRDLVQAMKRrvLELIQEKDRLWQRLQ 512
Cdd:COG1196   487 AEaaaRLLLLLEAEADYEGFLEGVKA--ALLLAGLRGLAGAVA 527
RUN_SNX29 cd17689
RUN domain found in sorting nexin-29 (SNX29) and similar proteins; SNX29, also called RUN ...
 17-163 6.32e-04

RUN domain found in sorting nexin-29 (SNX29) and similar proteins; SNX29, also called RUN domain-containing protein 2A (RUNDC2A), belongs to the sorting nexin family. Sorting nexins are a large group of proteins that are localized in the cytoplasm and have the potential for membrane association either through their lipid-binding PX domain, a phospholipid-binding motif, or through protein-protein interactions with membrane-associated protein complexes. Some sorting nexin family members have been shown to facilitate protein sorting. This model contains the RUN domain of SNX29.


Pssm-ID: 439051  Cd Length: 166  Bit Score: 40.68  E-value: 6.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327184  17 AAVSAILQGYGDGQGPVTDTSAELHRLCGCLELLLQFDQKEQKSFLGPRKDYWDFLCTALRRQRGNMEPI--HFVRSQ-- 92
Cdd:cd17689     4 DAVKQCQIRFGGKTELATESDSRVSCLCAQLEAVLQHGLKTSRSPNLVSSAVTQVSGLAGSLGSAETEPTfwPFVKEHlt 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327184  93 -------DKLK---TPLGKGRAFIRFCLARGQLAEALQLCLLNSELTREWYGPRSPLLCPERQEDILDSLYALNGVAFEL 162
Cdd:cd17689    84 khelerfELLKniwTDIGRGRAWLRSALNEHSLERYLHILLSNENLLRQYYEDWAFLRDEERSSMLPNMAAGLGSILFAL 163


                  .
gi 2217327184 163 D 163
Cdd:cd17689   164 S 164
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
412-520 8.07e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.21  E-value: 8.07e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327184  412 LQDEIKSLRLGLRKAEEQAQRQEQLLREQEGELQALR----------------EQLSRCQEERAELQA------QLEQKQ 469
Cdd:COG4913    615 LEAELAELEEELAEAEERLEALEAELDALQERREALQrlaeyswdeidvasaeREIAELEAELERLDAssddlaALEEQL 694

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2217327184  470 QEAERRDAMYQEELGGQRDLVQAMKRRVLELIQEKDRLWQRLQHLSSMAPE 520
Cdd:COG4913    695 EELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARL 745
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 393-483 8.53e-04

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 41.06  E-value: 8.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327184 393 QVQTEVTLVARREEQ-AEVSLQDEIKSLRLGLRKAEEQAQRQEQLLREQEGELQALREQLSRCQEERAELQAQLEQKQQE 471
Cdd:COG1579    67 EIEEVEARIKKYEEQlGNVRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAE 146

                          90
                  ....*....|..
gi 2217327184 472 AERRDAMYQEEL 483
Cdd:COG1579   147 LDEELAELEAEL 158
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
428-517 9.22e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.06  E-value: 9.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327184 428 EQAQRQEQLLREQEGELQALREQLSRCQEERAELQAQLEQKQQEAERRDAmyQEELGGQRDLVQAMKRRVLELIQEKDRL 507
Cdd:COG4717    74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEK--LLQLLPLYQELEALEAELAELPERLEEL 151

                          90
                  ....*....|
gi 2217327184 508 WQRLQHLSSM 517
Cdd:COG4717   152 EERLEELREL 161
TPR_MLP1_2 pfam07926
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ...
 410-512 1.00e-03

TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.


Pssm-ID: 462316 [Multi-domain]  Cd Length: 129  Bit Score: 39.16  E-value: 1.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327184 410 VSLQDEIKSLRLGLRKAEEQAQRQEQLLREQEG---------------------ELQALREQLSRCQEERAELQAQ---- 464
Cdd:pfam07926   4 SSLQSEIKRLKEEAADAEAQLQKLQEDLEKQAEiareaqqnyerelvlhaedikALQALREELNELKAEIAELKAEaesa 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2217327184 465 ---LEQKQQEAERRDAMYQEELggqrdlvQAMKRRVLELIQEKDRLWQRLQ 512
Cdd:pfam07926  84 kaeLEESEESWEEQKKELEKEL-------SELEKRIEDLNEQNKLLHDQLE 127
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 404-518 1.02e-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: 41.98  E-value: 1.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327184  404 REEQAEV-SLQDEIKSLRLGLRKAEEQAQRQEQLLREQEGELQALREQLSRCQEERAELQAQLEQKQQEAERRDamyqEE 482
Cdd:TIGR02169  346 EEERKRRdKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLS----EE 421

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 2217327184  483 LGGQRDLVQAMKRRVLELIQEKD----RLWQRLQHLSSMA 518
Cdd:TIGR02169  422 LADLNAAIAGIEAKINELEEEKEdkalEIKKQEWKLEQLA 461
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 403-510 1.04e-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: 41.86  E-value: 1.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327184 403 RREEQAEVSLQDEIKSLRLGLRKAEEQAQRQEQLLREQEGELQALREQLSRCQEE--RAELQAQLEQKQQEAERRDAMYQ 480
Cdd:pfam15709 373 KMREELELEQQRRFEEIRLRKQRLEEERQRQEEEERKQRLQLQAAQERARQQQEEfrRKLQELQRKKQQEEAERAEAEKQ 452

                          90       100       110
                  ....*....|....*....|....*....|
gi 2217327184 481 EELGGQRDLVQAMKrRVLELIQEKDRLWQR 510
Cdd:pfam15709 453 RQKELEMQLAEEQK-RLMEMAEEERLEYQR 481
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
402-500 1.11e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.68  E-value: 1.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327184 402 ARREEQAEVSLQDEIKSLRLGLRKAEEQAQRQEQLLR-EQEGELQALREQLSRCQEERAELQAQLEQKQQEAERRDAmyQ 480
Cdd:COG4717   151 LEERLEELRELEEELEELEAELAELQEELEELLEQLSlATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEE--E 228

                          90       100
                  ....*....|....*....|
gi 2217327184 481 EELGGQRDLVQAMKRRVLEL 500
Cdd:COG4717   229 LEQLENELEAAALEERLKEA 248
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 391-506 1.13e-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: 41.97  E-value: 1.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327184  391 NPQVQTEVTLVARREEQAEvSLQDEIKSLRLGLRKAEEQAQRQEQLLREQEGELQALREQLSRCQEERAELQAQLEQKQQ 470
Cdd:TIGR02168  858 AAEIEELEELIEELESELE-ALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEV 936

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 2217327184  471 EAERRDAMYQEELGGQRDLVQAMKRRVLELIQEKDR 506
Cdd:TIGR02168  937 RIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARR 972
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 395-513 1.13e-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: 41.97  E-value: 1.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327184  395 QTEVTLVARREEQAEV---SLQDEIKSLRLGLRKAEEQAQRQEQLLREQEGELQALREQLSRCQEERAELQAQLEQKQQE 471
Cdd:TIGR02168  336 AEELAELEEKLEELKEeleSLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDR 415

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 2217327184  472 AERRDamyQEELGGQRDLVQAMKRRVLELIQEKDRLWQRLQH 513
Cdd:TIGR02168  416 RERLQ---QEIEELLKKLEEAELKELQAELEELEEELEELQE 454
PRK09039 PRK09039
peptidoglycan -binding protein;
405-506 1.14e-03

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 41.10  E-value: 1.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327184 405 EEQAEVSLQDEIKSLRLGLRKAEEQAQRQEQLLREQEGELQALREQLsrcqeerAELQAQLEQKQQEAERrdAMYQEELG 484
Cdd:PRK09039   72 ERQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRA-------GELAQELDSEKQVSAR--ALAQVELL 142

                          90       100
                  ....*....|....*....|....*...
gi 2217327184 485 GQRdlVQAMKRR------VLELIQEKDR 506
Cdd:PRK09039  143 NQQ--IAALRRQlaaleaALDASEKRDR 168
PTZ00121 PTZ00121
MAEBL; Provisional
 402-499 1.22e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.05  E-value: 1.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327184  402 ARREEQAEVSLQDeikslrlgLRKAEEQAQRQEQLLREQEGELQAlREQLSRCQEERAELQAQLEQKQQEAERRDAMYQE 481
Cdd:PTZ00121  1612 AKKAEEAKIKAEE--------LKKAEEEKKKVEQLKKKEAEEKKK-AEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKK 1682

                           90
                   ....*....|....*...
gi 2217327184  482 ELGGQRDLVQAMKRRVLE 499
Cdd:PTZ00121  1683 AEEDEKKAAEALKKEAEE 1700
DUF4659 pfam15558
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ...
 401-513 1.31e-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: 41.18  E-value: 1.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327184 401 VARREEQAEVSLQDEIKSLRLGLRKAEEQA----QRQEQLLREQEGELQALREQLSRCQEER---AELQAQLEQKQQEAE 473
Cdd:pfam15558  89 VIEKESRWREQAEDQENQRQEKLERARQEAeqrkQCQEQRLKEKEEELQALREQNSLQLQERleeACHKRQLKEREEQKK 168

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2217327184 474 RRDAMYQEELGGQRDLVQAMKRRVLELIQEKDRLWQRLQH 513
Cdd:pfam15558 169 VQENNLSELLNHQARKVLVDCQAKAEELLRRLSLEQSLQR 208
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
393-503 1.71e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.29  E-value: 1.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327184 393 QVQTEVTLVARREEqAEVSLQDEIKSLRLGLRKAEEQAQRQEqlLREQEGELQALREQLSRCQEERAELQAQLEQKQQEA 472
Cdd:COG4717   393 QAEEYQELKEELEE-LEEQLEELLGELEELLEALDEEELEEE--LEELEEELEELEEELEELREELAELEAELEQLEEDG 469

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2217327184 473 ERRDAMYQEELGGQRDLVQAMKRRVLELIQE 503
Cdd:COG4717   470 ELAELLQELEELKAELRELAEEWAALKLALE 500
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
400-502 1.73e-03

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 41.16  E-value: 1.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327184 400 LVARREEQAEVSLQDEIKSLRLGLRKAEEQAQRQEQLLREQEGELQALREQL----SRCQEERAELQAQLEQKQQEAERR 475
Cdd:COG3206   249 LGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIaalrAQLQQEAQRILASLEAELEALQAR 328

                          90       100
                  ....*....|....*....|....*..
gi 2217327184 476 DAMYQEELGGQRDLVQAMKRRVLELIQ 502
Cdd:COG3206   329 EASLQAQLAQLEARLAELPELEAELRR 355
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 393-477 1.76e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 40.90  E-value: 1.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327184 393 QVQTEVTLVARREEQAEVSLQDEIKSLRLGLRKAEEQAQRQEQLLREQEGELQALREQLSRCQEERAELQAQLEQKQQEA 472
Cdd:COG4942   157 ADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236


                  ....*
gi 2217327184 473 ERRDA 477
Cdd:COG4942   237 AAAAE 241
hsdR PRK11448
type I restriction enzyme EcoKI subunit R; Provisional
 385-520 1.77e-03

type I restriction enzyme EcoKI subunit R; Provisional


Pssm-ID: 236912 [Multi-domain]  Cd Length: 1123  Bit Score: 41.09  E-value: 1.77e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327184  385 EDSTVENPQVQTEV-TLVARREEQAEVSLQDEIKslrlgLRKAEEQAQRQEQLLREQEGELQALREQLsrcqeerAELQA 463
Cdd:PRK11448   138 EDPENLLHALQQEVlTLKQQLELQAREKAQSQAL-----AEAQQQELVALEGLAAELEEKQQELEAQL-------EQLQE 205

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217327184  464 QLEQKQQEAERRDAMYQEELGGQRDLVQAMKRRvleLI--QEKDRLW----QRLQHLSSMAPE 520
Cdd:PRK11448   206 KAAETSQERKQKRKEITDQAAKRLELSEEETRI---LIdqQLRKAGWeadsKTLRFSKGARPE 265
PRK12704 PRK12704
phosphodiesterase; Provisional
 403-482 1.86e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 40.92  E-value: 1.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327184 403 RREEQAEVSLQ-DEIKSLRLGLRKAEEQAQRQEQLLREQEGELQALREQLSRCQEERAELQAQLEQKQ----QEAERRDA 477
Cdd:PRK12704   70 RNEFEKELRERrNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIeeqlQELERISG 149


                  ....*
gi 2217327184 478 MYQEE 482
Cdd:PRK12704  150 LTAEE 154
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
423-513 1.92e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.91  E-value: 1.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327184 423 LRKAEEQAQRQEQLLREQEGELQALREQLSRCQEERAELQAQLEQKQQEAERRDAmYQEELGGQRDLVQAMKRrvLELIQ 502
Cdd:COG4717    76 LEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPL-YQELEALEAELAELPER--LEELE 152

                          90
                  ....*....|.
gi 2217327184 503 EKDRLWQRLQH 513
Cdd:COG4717   153 ERLEELRELEE 163
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 416-519 1.92e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 40.52  E-value: 1.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327184 416 IKSLRLGLRKAEEQAQRQEQLLREQEGELQALREQLSRCQEERAELQAQLEQKQQEAERRDAMYQEELGGQRDLVQAMKR 495
Cdd:COG4942   141 LKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQ 220

                          90       100
                  ....*....|....*....|....
gi 2217327184 496 RVLELIQEKDRLWQRLQHLSSMAP 519
Cdd:COG4942   221 EAEELEALIARLEAEAAAAAERTP 244
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 407-504 1.93e-03

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


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 40.25  E-value: 1.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327184 407 QAEVSLQDEIKSLRLgLRKAEEQAQRQEQLLREQEGELQALREQLSRCQEERAE-LQAQLEQKQQEAERR-DAMYQEELG 484
Cdd:cd16269   188 QADQALTEKEKEIEA-ERAKAEAAEQERKLLEEQQRELEQKLEDQERSYEEHLRqLKEKMEEERENLLKEqERALESKLK 266

                          90       100
                  ....*....|....*....|
gi 2217327184 485 GQRDLVQAMKRRVLELIQEK 504
Cdd:cd16269   267 EQEALLEEGFKEQAELLQEE 286
COG5493 COG5493
Uncharacterized protein, contains PD-(D/E)XK nuclease domain [General function prediction only] ...
 403-483 2.01e-03

Uncharacterized protein, contains PD-(D/E)XK nuclease domain [General function prediction only];


Pssm-ID: 444244 [Multi-domain]  Cd Length: 239  Bit Score: 39.97  E-value: 2.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327184 403 RREEQAEVSLQDEIKSLRLGLRKAEEQAQRQEQLLREQEGELQALREQLSRCQEERAELQAQlEQKQQEAERRDAMYQEE 482
Cdd:COG5493    23 RYAVLGLLATKDGLEELLERLEKLEEQMRKWEEQLRKLEEEIKKLREQVRKLEEDVKRLEEQ-ERKLEEAMAEHSELREE 101


                  .
gi 2217327184 483 L 483
Cdd:COG5493   102 L 102
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 411-492 2.60e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 40.20  E-value: 2.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327184 411 SLQDEIKSLRLGLRKAEEQAQRQEQLLREQEGELQALREQLSRCQEERAELQAQLEQKQQEAERR-DAMYQEelGGQRDL 489
Cdd:COG3883    27 ELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERaRALYRS--GGSVSY 104


                  ...
gi 2217327184 490 VQA 492
Cdd:COG3883   105 LDV 107
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 406-477 2.86e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 40.20  E-value: 2.86e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217327184 406 EQAEVSLQDEIKSLRLGLRKAEEQAQRQEQLLREQEGELQALREQLSRCQEERAELQAQLEQKQQEAERRDA 477
Cdd:COG3883   146 EAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAA 217
PTZ00491 PTZ00491
major vault protein; Provisional
 389-506 2.88e-03

major vault protein; Provisional


Pssm-ID: 240439 [Multi-domain]  Cd Length: 850  Bit Score: 40.39  E-value: 2.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327184 389 VENPQVQT-EVTLVARREE-QAEVSLQDEIKSlrlglrKAEEQAQRQEQLLREQE--GEL-------------------- 444
Cdd:PTZ00491  630 ITNVDVQSvEPVDERTRDSlQKSVQLAIEITT------KSQEAAARHQAELLEQEarGRLerqkmhdkakaeeqrtklle 703

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217327184 445 ------------QALREQLSRCQEERAELQAQLEQKQQEAERRDAMYQEELGGQRdlvqamKRRVLELIQEKDR 506
Cdd:PTZ00491  704 lqaesaavessgQSRAEALAEAEARLIEAEAEVEQAELRAKALRIEAEAELEKLR------KRQELELEYEQAQ 771
RUN_RUBCN cd17686
RUN domain found in Run domain Beclin-1-interacting and cysteine-rich domain-containing ...
 40-169 3.14e-03

RUN domain found in Run domain Beclin-1-interacting and cysteine-rich domain-containing protein (RUBCN) and similar proteins; RUBCN, also called rubicon, or beclin-1 associated RUN domain containing protein (Baron), is part of a Beclin-1-Vps34-containing autophagy complex. It negatively regulates endosome maturation and degradative endocytic trafficking and impairs autophagosome maturation process. It is also an important negative regulator of the innate immune response, enhances viral replication and may play a role in viral immune evasion. This model contains the RUN domain of RUBCN.


Pssm-ID: 439048  Cd Length: 151  Bit Score: 38.40  E-value: 3.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327184  40 LHRLCGCLELLLQFDQKEQKSfLGPRKDYWDFLCTALRRQRGNMEPIHFVRSQDKLKTP-LGKGRAFIRFCLARGQLAEA 118
Cdd:cd17686    21 LQRLCRAVENILQHGLKEFQG-LNKEIDDWEFVQGLRWLQPTLAPSIEQQSRSSPSESEvSDKGRLWLRQSLQQHCLSSQ 99

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2217327184 119 LQLCLLNSELTREWYGPRSPLLCPERQEDILDSLyalngVAFELDlqQPDL 169
Cdd:cd17686   100 LQWLVSDKELLRKYYEDEAFLRQEGYATALLICL-----TAVELN--QPSL 143
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
395-511 3.22e-03

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 40.39  E-value: 3.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327184 395 QTEVTLVARREEQAEVSLQDEIKSLRLGLRKAEEQAQRQEQLLREQEGELQALREQLSRCQEERAELQA-----QLEQKQ 469
Cdd:COG3206   193 EAEAALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQspviqQLRAQL 272

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2217327184 470 QEAERRDAMYQEELGGQRDLVQAMKRRVLELIQEKDRLWQRL 511
Cdd:COG3206   273 AELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRI 314
Golgin_A5 pfam09787
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ...
 384-516 3.30e-03

Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.


Pssm-ID: 462900 [Multi-domain]  Cd Length: 305  Bit Score: 39.74  E-value: 3.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327184 384 KEDSTVENPQVQTEVTLVA-----RREEQAE--VSLQDEIKSLRLGLRKAEEQAQRQEQLLREQegeLQALREQLSRCQE 456
Cdd:pfam09787  31 KEGSGVEGLDSSTALTLELeelrqERDLLREeiQKLRGQIQQLRTELQELEAQQQEEAESSREQ---LQELEEQLATERS 107

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217327184 457 ERAELQAQLEQKQQEAERrdamYQEELGGQRDLVQA-MKRRVLELIQEKDRLWQRLQHLSS 516
Cdd:pfam09787 108 ARREAEAELERLQEELRY----LEEELRRSKATLQSrIKDREAEIEKLRNQLTSKSQSSSS 164
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 378-520 3.86e-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: 40.04  E-value: 3.86e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327184  378 LQGHATKEDSTVENPQVQTE------VTLVARREEQAE--VSLQDEIKSLRLGLRKAEEQAQRQEQLLREQEGELQALRE 449
Cdd:TIGR02168  815 LNEEAANLRERLESLERRIAaterrlEDLEEQIEELSEdiESLAAEIEELEELIEELESELEALLNERASLEEALALLRS 894

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217327184  450 QLsrcqEERAELQAQLEQKQQEAERrdamyqeELGGQRDLVQAMKRRVLELIQEKDRLWQRLQHLSSMAPE 520
Cdd:TIGR02168  895 EL----EELSEELRELESKRSELRR-------ELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLE 954
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
401-515 4.09e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.02  E-value: 4.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327184 401 VARREEQAEVSLQD---EIKSLRLGLRKAEEQAQRQEQLLREQEGELQALREQLSRCQEERAELQAQLEqkqqEAERRDA 477
Cdd:PRK02224  326 LRDRLEECRVAAQAhneEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIE----ELRERFG 401

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2217327184 478 MYQEELGGQRDLVQamkrrvlELIQEKDRLWQRLQHLS 515
Cdd:PRK02224  402 DAPVDLGNAEDFLE-------ELREERDELREREAELE 432
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 411-495 4.51e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 39.43  E-value: 4.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327184 411 SLQDEIKSLRLGLRKAEEQAQRQEQLLREQEGELQALREQLSRCQEERAELQAQLEQKQQEAERRdamyQEELGgqrDLV 490
Cdd:COG3883    20 AKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEER----REELG---ERA 92


                  ....*
gi 2217327184 491 QAMKR 495
Cdd:COG3883    93 RALYR 97
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 412-475 4.55e-03

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 214922 [Multi-domain]  Cd Length: 140  Bit Score: 37.56  E-value: 4.55e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217327184  412 LQDEIKSLRLGLRKAEEQAQRQEQLL-----REQEGELQALREQLsrcQEERAELQAQLEQKQQEAERR 475
Cdd:smart00935  30 RQAELEKLEKELQKLKEKLQKDAATLseaarEKKEKELQKKVQEF---QRKQQKLQQDLQKRQQEELQK 95
HAUS2 pfam15003
HAUS augmin-like complex subunit 2; This family of proteins is found in eukaryotes. Proteins ...
 444-512 4.78e-03

HAUS augmin-like complex subunit 2; This family of proteins is found in eukaryotes. Proteins in this family are typically between 203 and 291 amino acids in length. HAUS augmin-like complex subunit 2 is alternatively called centrosomal protein of 27 kDa (CEP27). It localized in the microtubule organizing centre, the centrosome. These microtubules are part of the cytoskeleton and give the cell its shape, provides it with a platform for motility and are crucial for mitosis. This protein is part of the HAUS augmin-like complex. This interacts with the gamma-tubulin ring complex (gamma-TuRC) which is required for spindle generation. HAUS2 may also increase the tension between spindle and kinetochore allowing for chromosome segregation during mitosis. This protein is involved in mitotic spindle assembly, maintenance of centrosome integrity and completion of cytokinesis.


Pssm-ID: 373465  Cd Length: 191  Bit Score: 38.32  E-value: 4.78e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217327184 444 LQALReQLSRCQEERAELQAQLEQKQQEAERRDAMYQEELGGQRDLVQAMKRRVLELIQEKDRLWQRLQ 512
Cdd:pfam15003  41 ISRLR-ELSNVQRELAQLNLELQGRKDDKDTADLTHVSEIEKKCEALQRMTTHLKAVIQNKDRIIARLQ 108
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 393-515 5.07e-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: 39.65  E-value: 5.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327184  393 QVQTEVTLVARREEQAEVSL------QDEIKSLRLGLRKAEEQAQRQEQLLREQ----EGELQALREQLSRCQEERAELQ 462
Cdd:TIGR02168  681 ELEEKIEELEEKIAELEKALaelrkeLEELEEELEQLRKELEELSRQISALRKDlarlEAEVEQLEERIAQLSKELTELE 760

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2217327184  463 AQ---LEQKQQEAERRDAMYQEELGGQRDLVQAMKRRVLELIQEKDRLWQRLQHLS 515
Cdd:TIGR02168  761 AEieeLEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLN 816
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 402-475 5.12e-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: 37.21  E-value: 5.12e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217327184 402 ARREEQAEVSLQDEIKSLRLGLRKAEEQAQRQEQLLREQEGELQALREQLSRCQEERAELQAQLEQKQQEAERR 475
Cdd:pfam20492  22 TKKAQEELEESEETAEELEEERRQAEEEAERLEQKRQEAEEEKERLEESAEMEAEEKEQLEAELAEAQEEIARL 95
DUF4686 pfam15742
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ...
 402-514 5.63e-03

Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins in this family are typically between 498 and 775 amino acids in length. There is a conserved DLK sequence motif.


Pssm-ID: 464838 [Multi-domain]  Cd Length: 384  Bit Score: 39.28  E-value: 5.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327184 402 ARREEQAEVSLQDEIKSLRLGLRKAEEQAQRQEQLLREQEGEL-QALREQLSRCQEERAELQaqleqkQQEAERRDAmyQ 480
Cdd:pfam15742 163 ASENEAKLKQQYQEEQQKRKLLDQNVNELQQQVRSLQDKEAQLeMTNSQQQLRIQQQEAQLK------QLENEKRKS--D 234

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2217327184 481 EELGGQRDLvqamKRRVLELIQEKDRLWQRLQHL 514
Cdd:pfam15742 235 EHLKSNQEL----SEKLSSLQQEKEALQEELQQV 264
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 397-516 5.66e-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: 5.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327184  397 EVTLVARREEQAEVS---LQDEIKSLRLGLRKAEEQAQRQEQLLREQEGELQALREQLSRCQEERAELQAQL-EQKQQEA 472
Cdd:TIGR02169  771 EEDLHKLEEALNDLEarlSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRiDLKEQIK 850

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 2217327184  473 ERRDAmyQEELGGQrdlVQAMKRRVLELIQEKDRLWQRLQHLSS 516
Cdd:TIGR02169  851 SIEKE--IENLNGK---KEELEEELEELEAALRDLESRLGDLKK 889
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 422-481 5.75e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 39.02  E-value: 5.75e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217327184 422 GLRKAEEQAQRQEQ-----LLREQEGELQALREQlsrcqeERAELQAQLEQKQQEAERRDAMYQE 481
Cdd:PRK09510   73 SAKRAEEQRKKKEQqqaeeLQQKQAAEQERLKQL------EKERLAAQEQKKQAEEAAKQAALKQ 131
LCD1 pfam09798
DNA damage checkpoint protein; This is a family of proteins which regulate checkpoint kinases. ...
 412-499 6.13e-03

DNA damage checkpoint protein; This is a family of proteins which regulate checkpoint kinases. In Schizosaccharomyces pombe this protein is called Rad26 and in Saccharomyces cerevisiae it is called LCD1.


Pssm-ID: 462906  Cd Length: 615  Bit Score: 39.22  E-value: 6.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327184 412 LQDEIKSL-RLGLRKAEEQAQRQEQLLREQEGELQALREQLSRCQEERAELqaQLEQKQQEAERRDAMYQEELGGQRDLV 490
Cdd:pfam09798   2 LRDKLELLqQEKEKELEKLKNSYEELKSSHEEELEKLKQEVQKLEDEKKFL--LNELRSLSATSPASSQSHETDTDDSSS 79


                  ....*....
gi 2217327184 491 QAMKRRVLE 499
Cdd:pfam09798  80 VSLKKRKIE 88
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 411-520 6.14e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 38.98  E-value: 6.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327184 411 SLQDEIKSLRLGLRKAEEQAQRQEQLLREQEgELQALREQLSRCQEERAELQAQLEQKQQEAERRDAMYQEELGGQRDLV 490
Cdd:COG4942   130 DFLDAVRRLQYLKYLAPARREQAEELRADLA-ELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKEL 208

                          90       100       110
                  ....*....|....*....|....*....|
gi 2217327184 491 QAMKRRVLELIQEKDRLWQRLQHLSSMAPE 520
Cdd:COG4942   209 AELAAELAELQQEAEELEALIARLEAEAAA 238
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 384-507 6.61e-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: 39.27  E-value: 6.61e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327184  384 KEDSTVENPQVQTEVTLVARRE-EQAEVSLQDEIKSLRLGLRKAEEQAQ----RQEQLLREQEgELQALREQLSRCQEER 458
Cdd:TIGR02168  257 ELTAELQELEEKLEELRLEVSElEEEIEELQKELYALANEISRLEQQKQilreRLANLERQLE-ELEAQLEELESKLDEL 335

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 2217327184  459 AELQAQLEQKQQEAERRDAMYQEELGGQRDLVQAMKRRVLELIQEKDRL 507
Cdd:TIGR02168  336 AEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETL 384
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
 414-510 6.94e-03

Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.


Pssm-ID: 464001 [Multi-domain]  Cd Length: 200  Bit Score: 37.96  E-value: 6.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327184 414 DEIKSLRLGLRKAEEQAQRQEQLLREQEGELQALREQLSRCQEERAELQAQLEQ----KQ--QEAERRDAMYQEELGGQR 487
Cdd:pfam13851  26 ELIKSLKEEIAELKKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEELRKQLENyekdKQslKNLKARLKVLEKELKDLK 105

                          90       100
                  ....*....|....*....|...
gi 2217327184 488 DLVQAMKRRVLELIQEKDRLWQR 510
Cdd:pfam13851 106 WEHEVLEQRFEKVERERDELYDK 128
mukB PRK04863
chromosome partition protein MukB;
407-480 7.73e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 39.17  E-value: 7.73e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217327184  407 QAEVSLQDEIKSLRLGLRKAEEQAQRQEQLLREQEGELQALREQLSRCQEERAELQAQLEQKQQ---EAERRDAMYQ 480
Cdd:PRK04863   341 QTALRQQEKIERYQADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQaldVQQTRAIQYQ 417
OmpH pfam03938
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 412-472 8.74e-03

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 461098 [Multi-domain]  Cd Length: 140  Bit Score: 36.79  E-value: 8.74e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217327184 412 LQDEIKSLRLGLRKAEEQAQRQEQLL----REQEGELQALREQLsrcQEERAELQAQLEQKQQEA 472
Cdd:pfam03938  31 RQAELEAKQKELQKLYEELQKDGALLeeerEEKEQELQKKEQEL---QQLQQKAQQELQKKQQEL 92
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 424-499 9.33e-03

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: 38.95  E-value: 9.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327184 424 RKAEEQAQRQEQLLREQEG----ELQALREQ----LSRCQEERAELQAQLEQ-KQQEAER-RDAMYQEELGGQRDLVQAM 493
Cdd:pfam17380 413 RKIQQQKVEMEQIRAEQEEarqrEVRRLEEErareMERVRLEEQERQQQVERlRQQEEERkRKKLELEKEKRDRKRAEEQ 492


                  ....*.
gi 2217327184 494 KRRVLE 499
Cdd:pfam17380 493 RRKILE 498
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
412-516 9.52e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 38.34  E-value: 9.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327184 412 LQDEIKSLRLGLRKAEEQAQRQEQLLREQEGELQALREQLsrcQEERAELQAQLEQKQQEAERRDAMYQEELGGQRDLvQ 491
Cdd:COG4372    43 LQEELEQLREELEQAREELEQLEEELEQARSELEQLEEEL---EELNEQLQAAQAELAQAQEELESLQEEAEELQEEL-E 118

                          90       100
                  ....*....|....*....|....*
gi 2217327184 492 AMKRRVLELIQEKDRLWQRLQHLSS 516
Cdd:COG4372   119 ELQKERQDLEQQRKQLEAQIAELQS 143
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 400-512 9.72e-03

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 38.87  E-value: 9.72e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217327184  400 LVARREEQAEV--SLQDEIKSLRLGLRKAEEQAQRQEQLLREQEGELQALREQLSRCQEERAELQAQLEQKQQEAERRDA 477
Cdd:TIGR00606  851 LIQDQQEQIQHlkSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELIS 930

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2217327184  478 MYQEELGGQRDLVQAMKRRVLELIQEKDRLWQRLQ 512
Cdd:TIGR00606  931 SKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQ 965
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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