NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|157738667|ref|NP_078789|]
View 

FYVE and coiled-coil domain-containing protein 1 isoform 1 [Homo sapiens]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
RUN_FYCO1 cd17698
RUN domain found in FYVE and coiled-coil domain-containing protein 1 (FYCO1) and similar ...
 7-164 7.98e-103

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: 324.34  E-value: 7.98e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667    7 ESQLQRIIRDLQDAVTELSKEFQEAGEPITDDSTSLHKFSYKLEYLLQFDQKEKATLLGNKKDYWDYFCACLAKVKGAND 86
Cdd:cd17698     1 ESQLQKIIRDLQDCVTELKKEFEETGEPITDDSTTLHKFCAKLEYLLQFDQKEKTTLLGGRKDYWDYFCECLAKVKGLND 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157738667   87 GIRFVKSISELRTSLGKGRAFIRYSLVHQRLADTLQQCFMNTKVTSDWYYARSPFLQPKLSSDIVGQLYELTEVQFDL 164
Cdd:cd17698    81 GIRFVKSLKEVRTSLGKGRAFIRYSLVHQRLADTLQQCVMNGKVTSDWYYPRSVFLNHKYSSDIINSLYDLNEVQFDL 158
FYVE_FYCO1 cd15726
FYVE domain found in FYVE and coiled-coil domain-containing protein 1 (FYCO1) and similar ...
 1170-1227 9.91e-37

FYVE domain found in FYVE and coiled-coil domain-containing protein 1 (FYCO1) and similar proteins; FYCO1, also termed zinc finger FYVE domain-containing protein 7, is a phosphatidylinositol 3-phosphate (PtdIns3P or PI3P)-binding protein that is associated with the exterior of autophagosomes and mediates microtubule plus-end-directed vesicle transport. It acts as an effector of GTP-bound Rab7, a GTPase that recruits FYCO1 to autophagosomes and has been implicated in autophagosome-lysosomal fusion. FYCO1 also interacts with two microtubule motor proteins, kinesin (KIF) 5B and KIF23, and thus functions as a platform for assembly of vesicle fusion and trafficking factors. FYCO1 contains an N-terminal alpha-helical RUN domain followed by a long central coiled-coil region, a FYVE domain and a GOLD (Golgi dynamics) domain in C-terminus.


:

Pssm-ID: 277265 [Multi-domain]  Cd Length: 58  Bit Score: 132.68  E-value: 9.91e-37
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 157738667 1170 WLGDTEANHCLDCKREFSWMVRRHHCRICGRIFCYYCCNNYVLSKHGGKKERCCRACF 1227
Cdd:cd15726     1 WQDDTDVTHCLDCKSEFSWMVRRHHCRLCGRIFCYACSNFYVLTAHGGKKERCCKACF 58
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 243-1050 3.15e-29

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]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 127.48  E-value: 3.15e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   243 EVREKQLR---ERMQQLDRENQELRAAVSQQGEQLQTERERGRTAAEDNVRLTCLVAELQKQWEVTQATQNTVKELQTCL 319
Cdd:TIGR02168  221 ELRELELAllvLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRL 300

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   320 QGLELGAAEKEEDYHTALRRLESMLQPLAQELEATRDSLDKKNQHLASFPGWLAMAQQKADTASDTKGRQEPIPSDAAQE 399
Cdd:TIGR02168  301 EQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQ 380

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   400 MQELGEKLQALERERTKVEEVNRQQSAQLEQLVKELQ-LKEDARASLERLVK-EMAPLQEELSGKGQEADQLWRRLQELL 477
Cdd:TIGR02168  381 LETLRSKVAQLELQIASLNNEIERLEARLERLEDRRErLQQEIEELLKKLEEaELKELQAELEELEEELEELQEELERLE 460

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   478 AHTSSweeeLAELRREKKQQQEEKELLEQEVRSLTRQLQFLETQLAQVSQHVSDLEEQKKQLIQDKDHLSQQVGMLER-- 555
Cdd:TIGR02168  461 EALEE----LREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGye 536

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   556 ----LAGPPGPELPVAGEKNEALVPVNSSLQEAWGK------PEEEQRGLQEAQLDDTKVQEGSQE--EELRQANRELEK 623
Cdd:TIGR02168  537 aaieAALGGRLQAVVVENLNAAKKAIAFLKQNELGRvtflplDSIKGTEIQGNDREILKNIEGFLGvaKDLVKFDPKLRK 616

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   624 ELQNVVGRNQLLEGKLQALQadyqalQQRESAIQGSLASLEAEQASIRHL----GDQMEASLLA-------VRKAKEAMK 692
Cdd:TIGR02168  617 ALSYLLGGVLVVDDLDNALE------LAKKLRPGYRIVTLDGDLVRPGGVitggSAKTNSSILErrreieeLEEKIEELE 690

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   693 AQMAEKEAILQSKEGECQQLREEVEQCQQLAEARHRELRALESQCQQQTQLIEVLTAEKGQQgvgpptDNEARELAAQLA 772
Cdd:TIGR02168  691 EKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQL------SKELTELEAEIE 764

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   773 LSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAVLREHKTLVQQLkeqnealnrahvQELLQCSERE 852
Cdd:TIGR02168  765 ELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANL------------RERLESLERR 832

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   853 GALQEERADEAQQREEELRALQEELSqakcsseeaqLEHAELQEQLhrantdtAELGIQVCALTVEKERVEEALAcavqE 932
Cdd:TIGR02168  833 IAATERRLEDLEEQIEELSEDIESLA----------AEIEELEELI-------EELESELEALLNERASLEEALA----L 891

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   933 LQDAKEAASREREGLERQVAGLQQEKESLQEKLKAakaaagslpgLQAQLAQAEQRAQSLQEAAHQELNTLKFQLSAEIM 1012
Cdd:TIGR02168  892 LRSELEELSEELRELESKRSELRRELEELREKLAQ----------LELRLEGLEVRIDNLQERLSEEYSLTLEEAEALEN 961

                          810       820       830
                   ....*....|....*....|....*....|....*...
gi 157738667  1013 DYQSRLKNAGEECKSLRGQLEEQGRQLQAAEEAVEKLK 1050
Cdd:TIGR02168  962 KIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELK 999
GPCR_chapero_1 super family cl46312
GPCR-chaperone; This domain, and the associated ANK family repeat pfam00023 domain, together ...
 1419-1464 8.56e-04

GPCR-chaperone; This domain, and the associated ANK family repeat pfam00023 domain, together act as a chaperone for biogenesis and folding of the DP receptor for prostaglandin D2.


The actual alignment was detected with superfamily member pfam13897:

Pssm-ID: 480652  Cd Length: 133  Bit Score: 40.93  E-value: 8.56e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 157738667  1419 LIPTTRCNSHKENIQGQLKVRTPGIYMLIFDNTFSRFVSKKVFYHL 1464
Cdd:pfam13897   85 IVPVYRRDCHEEVYAGSHQYPGRGVYLLKFDNSYSLWRSKTLYYRV 130
YhaN super family cl34808
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
959-1169 1.78e-03

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


The actual alignment was detected with superfamily member COG4717:

Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.83  E-value: 1.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  959 ESLQEKLKAAKAAAGSLPGL---QAQLAQAEQRAQSLQEAAHQELNTLKFQLSAEIMDYQSRLKNAGEECKSLRgqleeq 1035
Cdd:COG4717    49 ERLEKEADELFKPQGRKPELnlkELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLE------ 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667 1036 grQLQAAEEAVEKLKATQADMgeklsctsNHLAECQAAMLRKDKEGAALREDLERTQKELEKATTKIQEYYNKLCQEVtn 1115
Cdd:COG4717   123 --KLLQLLPLYQELEALEAEL--------AELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLAT-- 190

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 157738667 1116 rERNDQKMLADLDDLNRTKKYLEERLIELLRDKDALWQKSDALEFQQKLSAEER 1169
Cdd:COG4717   191 -EEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEE 243
 
Name Accession Description Interval E-value
RUN_FYCO1 cd17698
RUN domain found in FYVE and coiled-coil domain-containing protein 1 (FYCO1) and similar ...
 7-164 7.98e-103

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: 324.34  E-value: 7.98e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667    7 ESQLQRIIRDLQDAVTELSKEFQEAGEPITDDSTSLHKFSYKLEYLLQFDQKEKATLLGNKKDYWDYFCACLAKVKGAND 86
Cdd:cd17698     1 ESQLQKIIRDLQDCVTELKKEFEETGEPITDDSTTLHKFCAKLEYLLQFDQKEKTTLLGGRKDYWDYFCECLAKVKGLND 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157738667   87 GIRFVKSISELRTSLGKGRAFIRYSLVHQRLADTLQQCFMNTKVTSDWYYARSPFLQPKLSSDIVGQLYELTEVQFDL 164
Cdd:cd17698    81 GIRFVKSLKEVRTSLGKGRAFIRYSLVHQRLADTLQQCVMNGKVTSDWYYPRSVFLNHKYSSDIINSLYDLNEVQFDL 158
FYVE_FYCO1 cd15726
FYVE domain found in FYVE and coiled-coil domain-containing protein 1 (FYCO1) and similar ...
 1170-1227 9.91e-37

FYVE domain found in FYVE and coiled-coil domain-containing protein 1 (FYCO1) and similar proteins; FYCO1, also termed zinc finger FYVE domain-containing protein 7, is a phosphatidylinositol 3-phosphate (PtdIns3P or PI3P)-binding protein that is associated with the exterior of autophagosomes and mediates microtubule plus-end-directed vesicle transport. It acts as an effector of GTP-bound Rab7, a GTPase that recruits FYCO1 to autophagosomes and has been implicated in autophagosome-lysosomal fusion. FYCO1 also interacts with two microtubule motor proteins, kinesin (KIF) 5B and KIF23, and thus functions as a platform for assembly of vesicle fusion and trafficking factors. FYCO1 contains an N-terminal alpha-helical RUN domain followed by a long central coiled-coil region, a FYVE domain and a GOLD (Golgi dynamics) domain in C-terminus.


Pssm-ID: 277265 [Multi-domain]  Cd Length: 58  Bit Score: 132.68  E-value: 9.91e-37
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 157738667 1170 WLGDTEANHCLDCKREFSWMVRRHHCRICGRIFCYYCCNNYVLSKHGGKKERCCRACF 1227
Cdd:cd15726     1 WQDDTDVTHCLDCKSEFSWMVRRHHCRLCGRIFCYACSNFYVLTAHGGKKERCCKACF 58
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 243-1050 3.15e-29

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: 127.48  E-value: 3.15e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   243 EVREKQLR---ERMQQLDRENQELRAAVSQQGEQLQTERERGRTAAEDNVRLTCLVAELQKQWEVTQATQNTVKELQTCL 319
Cdd:TIGR02168  221 ELRELELAllvLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRL 300

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   320 QGLELGAAEKEEDYHTALRRLESMLQPLAQELEATRDSLDKKNQHLASFPGWLAMAQQKADTASDTKGRQEPIPSDAAQE 399
Cdd:TIGR02168  301 EQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQ 380

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   400 MQELGEKLQALERERTKVEEVNRQQSAQLEQLVKELQ-LKEDARASLERLVK-EMAPLQEELSGKGQEADQLWRRLQELL 477
Cdd:TIGR02168  381 LETLRSKVAQLELQIASLNNEIERLEARLERLEDRRErLQQEIEELLKKLEEaELKELQAELEELEEELEELQEELERLE 460

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   478 AHTSSweeeLAELRREKKQQQEEKELLEQEVRSLTRQLQFLETQLAQVSQHVSDLEEQKKQLIQDKDHLSQQVGMLER-- 555
Cdd:TIGR02168  461 EALEE----LREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGye 536

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   556 ----LAGPPGPELPVAGEKNEALVPVNSSLQEAWGK------PEEEQRGLQEAQLDDTKVQEGSQE--EELRQANRELEK 623
Cdd:TIGR02168  537 aaieAALGGRLQAVVVENLNAAKKAIAFLKQNELGRvtflplDSIKGTEIQGNDREILKNIEGFLGvaKDLVKFDPKLRK 616

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   624 ELQNVVGRNQLLEGKLQALQadyqalQQRESAIQGSLASLEAEQASIRHL----GDQMEASLLA-------VRKAKEAMK 692
Cdd:TIGR02168  617 ALSYLLGGVLVVDDLDNALE------LAKKLRPGYRIVTLDGDLVRPGGVitggSAKTNSSILErrreieeLEEKIEELE 690

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   693 AQMAEKEAILQSKEGECQQLREEVEQCQQLAEARHRELRALESQCQQQTQLIEVLTAEKGQQgvgpptDNEARELAAQLA 772
Cdd:TIGR02168  691 EKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQL------SKELTELEAEIE 764

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   773 LSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAVLREHKTLVQQLkeqnealnrahvQELLQCSERE 852
Cdd:TIGR02168  765 ELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANL------------RERLESLERR 832

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   853 GALQEERADEAQQREEELRALQEELSqakcsseeaqLEHAELQEQLhrantdtAELGIQVCALTVEKERVEEALAcavqE 932
Cdd:TIGR02168  833 IAATERRLEDLEEQIEELSEDIESLA----------AEIEELEELI-------EELESELEALLNERASLEEALA----L 891

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   933 LQDAKEAASREREGLERQVAGLQQEKESLQEKLKAakaaagslpgLQAQLAQAEQRAQSLQEAAHQELNTLKFQLSAEIM 1012
Cdd:TIGR02168  892 LRSELEELSEELRELESKRSELRRELEELREKLAQ----------LELRLEGLEVRIDNLQERLSEEYSLTLEEAEALEN 961

                          810       820       830
                   ....*....|....*....|....*....|....*...
gi 157738667  1013 DYQSRLKNAGEECKSLRGQLEEQGRQLQAAEEAVEKLK 1050
Cdd:TIGR02168  962 KIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELK 999
FYVE pfam01363
FYVE zinc finger; The FYVE zinc finger is named after four proteins that it has been found in: ...
 1169-1232 4.23e-25

FYVE zinc finger; The FYVE zinc finger is named after four proteins that it has been found in: Fab1, YOTB/ZK632.12, Vac1, and EEA1. The FYVE finger has been shown to bind two Zn++ ions. The FYVE finger has eight potential zinc coordinating cysteine positions. Many members of this family also include two histidines in a motif R+HHC+XCG, where + represents a charged residue and X any residue. We have included members which do not conserve these histidine residues but are clearly related.


Pssm-ID: 426221 [Multi-domain]  Cd Length: 68  Bit Score: 99.76  E-value: 4.23e-25
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157738667  1169 RWLGDTEANHCLDCKREFSWMVRRHHCRICGRIFCYYCCNNYVL---SKHGGKKERCCRACFQKLSE 1232
Cdd:pfam01363    2 VWVPDSSATVCMICSKPFTFFRRRHHCRNCGRVFCSACSSKKISllpELGSNKPVRVCDACYDTLQK 68
FYVE smart00064
Protein present in Fab1, YOTB, Vac1, and EEA1; The FYVE zinc finger is named after four ...
 1169-1231 2.31e-24

Protein present in Fab1, YOTB, Vac1, and EEA1; The FYVE zinc finger is named after four proteins where it was first found: Fab1, YOTB/ZK632.12, Vac1, and EEA1. The FYVE finger has been shown to bind two Zn2+ ions. The FYVE finger has eight potential zinc coordinating cysteine positions. The FYVE finger is structurally related to the PHD finger and the RING finger. Many members of this family also include two histidines in a motif R+HHC+XCG, where + represents a charged residue and X any residue. The FYVE finger functions in the membrane recruitment of cytosolic proteins by binding to phosphatidylinositol 3-phosphate (PI3P), which is prominent on endosomes. The R+HHC+XCG motif is critical for PI3P binding.


Pssm-ID: 214499 [Multi-domain]  Cd Length: 68  Bit Score: 97.50  E-value: 2.31e-24
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157738667   1169 RWLGDTEANHCLDCKREFSWMVRRHHCRICGRIFCYYCCNNYVLSKHGG--KKERCCRACFQKLS 1231
Cdd:smart00064    3 HWIPDEEVSNCMGCGKEFNLTKRRHHCRNCGRIFCSKCSSKKAPLPKLGieRPVRVCDDCYENLN 67
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 589-1099 3.61e-22

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 104.25  E-value: 3.61e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  589 EEEQRGLQEAQLDDTKVQEGSQEEELRQANRELEKELQNVVGRNQLLEGKLQALQADYQALQQRESAIQGSLASLEAEQA 668
Cdd:COG1196   247 ELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELA 326

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  669 SIRHLGDQMEASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEV-EQCQQLAEARHRELRALESQCQQQTQLIEVL 747
Cdd:COG1196   327 ELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELaEAEEELEELAEELLEALRAAAELAAQLEELE 406

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  748 TAEKGQQgvgpptDNEARELAAQLALSQAQLEVHQGEVQRLQAqvvdLQAKMRAALDDQDKVQSQLSMAEAVLREHKTLV 827
Cdd:COG1196   407 EAEEALL------ERLERLEEELEELEEALAELEEEEEEEEEA----LEEAAEEEAELEEEEEALLELLAELLEEAALLE 476

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  828 QQLKEQNEALNRAHVQELLQCSEREGALQEERADEAQQREEELRALQEELSQ-AKCSSEEAQLEHAELQEQLHRANTDTA 906
Cdd:COG1196   477 AALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVlIGVEAAYEAALEAALAAALQNIVVEDD 556

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  907 ELGIQVCALTVEKERVEEALACAVQELQDAKEAASREREGLERQVAGLQQEKESLQEKLKAAKAAAGSLPGLQAQLAQAE 986
Cdd:COG1196   557 EVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAAL 636

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  987 QRAQSLQEAAHQELNTLKFQLSAEIMDYQSRLKNAGEEcKSLRGQLEEQGRQLQAAEEAVEKLKATQADMGEKLSCTSNH 1066
Cdd:COG1196   637 RRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAAL-LEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEE 715

                         490       500       510
                  ....*....|....*....|....*....|...
gi 157738667 1067 LAECQAAMLRKDKEGAALREDLERTQKELEKAT 1099
Cdd:COG1196   716 RLEEELEEEALEEQLEAEREELLEELLEEEELL 748
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 619-1183 6.68e-13

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: 74.00  E-value: 6.68e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   619 RELEKELQNVVGRNQLLEGKLQALQADYQ-----ALQQRESAIQGSLASLEAEQASIRHLGDQMEASLLAVRKAKEAMKA 693
Cdd:pfam15921  227 RELDTEISYLKGRIFPVEDQLEALKSESQnkielLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQE 306

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   694 QMAEKEAI----LQSKEGECQQLREEVEQCQQLAEARHRELRalESQCQQQTQLIEVLTAEKGQQGVGPPTDNEARELAA 769
Cdd:pfam15921  307 QARNQNSMymrqLSDLESTVSQLRSELREAKRMYEDKIEELE--KQLVLANSELTEARTERDQFSQESGNLDDQLQKLLA 384

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   770 -------QLALSQAQ---------------------LEVHQGEVQRLQAQVVDLQAKMRAALDDQdkvQSQLSMAEAVLR 821
Cdd:pfam15921  385 dlhkrekELSLEKEQnkrlwdrdtgnsitidhlrreLDDRNMEVQRLEALLKAMKSECQGQMERQ---MAAIQGKNESLE 461

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   822 EHKTLVQQLKEQNEALnRAHVQEL------LQCSERE-----GALQE-ERADEAQQRE------------EELRALQEE- 876
Cdd:pfam15921  462 KVSSLTAQLESTKEML-RKVVEELtakkmtLESSERTvsdltASLQEkERAIEATNAEitklrsrvdlklQELQHLKNEg 540

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   877 --LSQAKCSSEEAQLEHAE-------LQEQLHRANTDTAELGIQVCALTVEKERVEEALACAVQELQ------DAKEAAS 941
Cdd:pfam15921  541 dhLRNVQTECEALKLQMAEkdkvieiLRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQefkilkDKKDAKI 620

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   942 REregLERQVAGLQQEKESLqeklkaakAAAGSlPGLQAQLAQAEQRAQSLQEA--AHQELNTLkfqlSAEIMDYQSRLK 1019
Cdd:pfam15921  621 RE---LEARVSDLELEKVKL--------VNAGS-ERLRAVKDIKQERDQLLNEVktSRNELNSL----SEDYEVLKRNFR 684

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  1020 NAGEECKSLRGQLEeqgRQLQAAEEAVEKLKATQADMgeklSCTSNHLAECQAAMLRKDKEGAALREDLERTQKELEKAT 1099
Cdd:pfam15921  685 NKSEEMETTTNKLK---MQLKSAQSELEQTRNTLKSM----EGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAM 757

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  1100 TK-------IQEYYNKLCQEVTNRERNDQKMLADLDDLNRTKKYLEERL--IELLRDKDALwQKSDALEFQQKLSAEERW 1170
Cdd:pfam15921  758 TNankekhfLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVanMEVALDKASL-QFAECQDIIQRQEQESVR 836

                          650
                   ....*....|...
gi 157738667  1171 LgdtEANHCLDCK 1183
Cdd:pfam15921  837 L---KLQHTLDVK 846
mukB PRK04863
chromosome partition protein MukB;
584-962 2.33e-12

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 72.30  E-value: 2.33e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  584 AWGKPEEEQRGLQEAQLddtkvqegSQEEELRQANRELEKE---LQNVVGRNQLLEGKLQALQADYQALQQRESAIQGSL 660
Cdd:PRK04863  273 DYMRHANERRVHLEEAL--------ELRRELYTSRRQLAAEqyrLVEMARELAELNEAESDLEQDYQAASDHLNLVQTAL 344

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  661 ASLEAE---QASIRHLGDQMEASLLAVRKAKEamkaQMAEKEAILQSKEGECQQLREEVEQCQQLAEARHRE-------L 730
Cdd:PRK04863  345 RQQEKIeryQADLEELEERLEEQNEVVEEADE----QQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRaiqyqqaV 420

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  731 RALESqCQQQTQL-----------IEVLTAEKGQQgvgpptDNEARELAAQLALSQAQLEVHQ----------GEVQRLQ 789
Cdd:PRK04863  421 QALER-AKQLCGLpdltadnaedwLEEFQAKEQEA------TEELLSLEQKLSVAQAAHSQFEqayqlvrkiaGEVSRSE 493

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  790 AQVVdlqakMRAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNEAlnrahvQELLQCSEREGALQEERADEAQQREEE 869
Cdd:PRK04863  494 AWDV-----ARELLRRLREQRHLAEQLQQLRMRLSELEQRLRQQQRA------ERLLAEFCKRLGKNLDDEDELEQLQEE 562

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  870 LRALQEELSQAKCSSEEAQLEHAELQEQL--------------HRANTDTAELGIQVCALTVEKERVEEALacavQELQD 935
Cdd:PRK04863  563 LEARLESLSESVSEARERRMALRQQLEQLqariqrlaarapawLAAQDALARLREQSGEEFEDSQDVTEYM----QQLLE 638

                         410       420
                  ....*....|....*....|....*..
gi 157738667  936 AKEAASREREGLERQVAGLQQEKESLQ 962
Cdd:PRK04863  639 RERELTVERDELAARKQALDEEIERLS 665
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 939-1177 2.90e-07

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: 54.38  E-value: 2.90e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  939 AASREREGLERQVAGLQQEKESLQEKLKAAKAAAGSlpgLQAQLAQAEQRAQSLQEAAhQELNTLKFQLSAEIMDYQSRL 1018
Cdd:COG4942    17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKA---LLKQLAALERRIAALARRI-RALEQELAALEAELAELEKEI 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667 1019 KNAGEECKSLRGQLEEQGRQLQAAEEAVE-KLKATQAD------MGEKLSCTSNHLAECQAAMLRKDKEGAALREDLERT 1091
Cdd:COG4942    93 AELRAELEAQKEELAELLRALYRLGRQPPlALLLSPEDfldavrRLQYLKYLAPARREQAEELRADLAELAALRAELEAE 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667 1092 QKELEKATTKIQEYYNKLCQEVTNRERNdqkmladLDDLNRTKKYLEERLIELLRDKDALWQKSDALEFQQKLSAEERWL 1171
Cdd:COG4942   173 RAELEALLAELEEERAALEALKAERQKL-------LARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245


                  ....*.
gi 157738667 1172 GDTEAN 1177
Cdd:COG4942   246 AGFAAL 251
RUN pfam02759
RUN domain; This domain is present in several proteins that are linked to the functions of ...
 49-164 3.50e-06

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: 48.04  E-value: 3.50e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667    49 LEYLLQ------FDQKEKATLLGNKKDYWDYFCACLAKVKGANDGIRFVKSISELRT---SLGKGRAFIRYSLVHQRLAD 119
Cdd:pfam02759    6 LEALLShglkrsSLLILRAAGLLPERSFWALLERVGKLVPPAEELLSSVQELEQIHTpysPDGRGRAWIRLALNEKLLDQ 85

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 157738667   120 TLQQCFMNTKVTSDWYYARSPFLQPKLSSDIVGQLYELTEVQFDL 164
Cdd:pfam02759   86 WLKLLLSNKELLSEYYEPWALLADPEFGEILLGLLVGLSALDFNL 130
GOLD_2 pfam13897
Golgi-dynamics membrane-trafficking; Sec14-like Golgi-trafficking domain The GOLD domain is ...
 1419-1464 8.56e-04

Golgi-dynamics membrane-trafficking; Sec14-like Golgi-trafficking domain The GOLD domain is always found combined with lipid- or membrane-association domains.


Pssm-ID: 464028  Cd Length: 133  Bit Score: 40.93  E-value: 8.56e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 157738667  1419 LIPTTRCNSHKENIQGQLKVRTPGIYMLIFDNTFSRFVSKKVFYHL 1464
Cdd:pfam13897   85 IVPVYRRDCHEEVYAGSHQYPGRGVYLLKFDNSYSLWRSKTLYYRV 130
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 766-936 9.33e-04

Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.


Pssm-ID: 439154 [Multi-domain]  Cd Length: 309  Bit Score: 43.13  E-value: 9.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  766 ELAAQLALSQAQLEVhQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAVLREHKTLVQQLK--------EQNEAL 837
Cdd:cd22656    98 ELIDDLADATDDEEL-EEAKKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTALETLEkalkdlltDEGGAI 176

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  838 NRAHVQELLQcseregALQEERADEAQQREEELRALQEELsqakcSSEEAQLEHAE-LQEQLHRANTDTAELgiqvcalt 916
Cdd:cd22656   177 ARKEIKDLQK------ELEKLNEEYAAKLKAKIDELKALI-----ADDEAKLAAALrLIADLTAADTDLDNL-------- 237

                         170       180
                  ....*....|....*....|
gi 157738667  917 veKERVEEALAcAVQELQDA 936
Cdd:cd22656   238 --LALIGPAIP-ALEKLQGA 254
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
959-1169 1.78e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.83  E-value: 1.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  959 ESLQEKLKAAKAAAGSLPGL---QAQLAQAEQRAQSLQEAAHQELNTLKFQLSAEIMDYQSRLKNAGEECKSLRgqleeq 1035
Cdd:COG4717    49 ERLEKEADELFKPQGRKPELnlkELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLE------ 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667 1036 grQLQAAEEAVEKLKATQADMgeklsctsNHLAECQAAMLRKDKEGAALREDLERTQKELEKATTKIQEYYNKLCQEVtn 1115
Cdd:COG4717   123 --KLLQLLPLYQELEALEAEL--------AELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLAT-- 190

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 157738667 1116 rERNDQKMLADLDDLNRTKKYLEERLIELLRDKDALWQKSDALEFQQKLSAEER 1169
Cdd:COG4717   191 -EEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEE 243
PRK11281 PRK11281
mechanosensitive channel MscK;
978-1164 3.70e-03

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 41.82  E-value: 3.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  978 LQAQLAQAEQRAQ--SLQEAAHQELNTLKFQLsAEIMDYQSRLKnageeckSLRGQLEEQGRQLQAAEEAVEKLKATQAD 1055
Cdd:PRK11281   41 VQAQLDALNKQKLleAEDKLVQQDLEQTLALL-DKIDRQKEETE-------QLKQQLAQAPAKLRQAQAELEALKDDNDE 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667 1056 MGE-------------KLSCTSNHLAECQAAMLRKDKEGAALREDLERTQKELEKATTKIQEYYNKLCQEVTNRE--RND 1120
Cdd:PRK11281  113 ETRetlstlslrqlesRLAQTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANSQRLQQIRNLLKGGKVGGKalRPS 192

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 157738667 1121 QKM-----LADLD---DLNRTKKYLEERLIELLRDK-DALWQKSDALEFQQKL 1164
Cdd:PRK11281  193 QRVllqaeQALLNaqnDLQRKSLEGNTQLQDLLQKQrDYLTARIQRLEHQLQL 245
 
Name Accession Description Interval E-value
RUN_FYCO1 cd17698
RUN domain found in FYVE and coiled-coil domain-containing protein 1 (FYCO1) and similar ...
 7-164 7.98e-103

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: 324.34  E-value: 7.98e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667    7 ESQLQRIIRDLQDAVTELSKEFQEAGEPITDDSTSLHKFSYKLEYLLQFDQKEKATLLGNKKDYWDYFCACLAKVKGAND 86
Cdd:cd17698     1 ESQLQKIIRDLQDCVTELKKEFEETGEPITDDSTTLHKFCAKLEYLLQFDQKEKTTLLGGRKDYWDYFCECLAKVKGLND 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157738667   87 GIRFVKSISELRTSLGKGRAFIRYSLVHQRLADTLQQCFMNTKVTSDWYYARSPFLQPKLSSDIVGQLYELTEVQFDL 164
Cdd:cd17698    81 GIRFVKSLKEVRTSLGKGRAFIRYSLVHQRLADTLQQCVMNGKVTSDWYYPRSVFLNHKYSSDIINSLYDLNEVQFDL 158
RUN_RUFY4 cd17697
RUN domain found in RUN and FYVE domain-containing protein 4 (RUFY4) and similar proteins; ...
 15-164 3.72e-61

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: 205.80  E-value: 3.72e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   15 RDLQDAVTELSKEFQEAGEPITDDSTSLHKFSYKLEYLLQFDQKEKATLLGNKKDYWDYFCACLAKVKGANDGIRFVKSI 94
Cdd:cd17697     1 KDLQASIAELQKDQEEQQLPITDGSPELHRLCARLEYLLQFDQKEKKSFFGSRKDYWDFLCLCLNRHRGGTEGIHFVNST 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   95 SELRTSLGKGRAFIRYSLVHQRLADTLQQCFMNTKVTSDWYYARSPFLQPKLSSDIVGQLYELTEVQFDL 164
Cdd:cd17697    81 DKLKTPLGKGRAFIRYCLVQQQLAESLQLCLLNPELTGEWYYARSPFLSPELRSDILDSLYELNGVNFDL 150
RUN_RUFY4_like cd17682
RUN domain found in RUN and FYVE domain-containing protein 4 (RUFY4), FYVE and coiled-coil ...
 16-164 1.74e-53

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: 183.97  E-value: 1.74e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   16 DLQDAVTELSKEFqeaGEPITDDSTSLHKFSYKLEYLLQFDQKEKATLLGNKKDYWDYFCACLAKV----KGANDGIRFV 91
Cdd:cd17682     1 DLKGCVLDLKSEF---GEITDPDNPYLRPFCETLEKILRKGLKEKVSLGGRRKDYWDWLEELLKKLnkipKSLSDAVKFV 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157738667   92 KSISELRTSLGKGRAFIRYSLVHQRLADTLQQCFMNTKVTSDWYYARSPFLQPKLSSDIVGQLYELTEVQFDL 164
Cdd:cd17682    78 KSCKKVKTNQGRGRLFIRYALNKKCLHDPVQQLVKNPKLLSDYYSPDSILGNEILSEILLSLLYQLNEINFDL 150
FYVE_FYCO1 cd15726
FYVE domain found in FYVE and coiled-coil domain-containing protein 1 (FYCO1) and similar ...
 1170-1227 9.91e-37

FYVE domain found in FYVE and coiled-coil domain-containing protein 1 (FYCO1) and similar proteins; FYCO1, also termed zinc finger FYVE domain-containing protein 7, is a phosphatidylinositol 3-phosphate (PtdIns3P or PI3P)-binding protein that is associated with the exterior of autophagosomes and mediates microtubule plus-end-directed vesicle transport. It acts as an effector of GTP-bound Rab7, a GTPase that recruits FYCO1 to autophagosomes and has been implicated in autophagosome-lysosomal fusion. FYCO1 also interacts with two microtubule motor proteins, kinesin (KIF) 5B and KIF23, and thus functions as a platform for assembly of vesicle fusion and trafficking factors. FYCO1 contains an N-terminal alpha-helical RUN domain followed by a long central coiled-coil region, a FYVE domain and a GOLD (Golgi dynamics) domain in C-terminus.


Pssm-ID: 277265 [Multi-domain]  Cd Length: 58  Bit Score: 132.68  E-value: 9.91e-37
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 157738667 1170 WLGDTEANHCLDCKREFSWMVRRHHCRICGRIFCYYCCNNYVLSKHGGKKERCCRACF 1227
Cdd:cd15726     1 WQDDTDVTHCLDCKSEFSWMVRRHHCRLCGRIFCYACSNFYVLTAHGGKKERCCKACF 58
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 243-1050 3.15e-29

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: 127.48  E-value: 3.15e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   243 EVREKQLR---ERMQQLDRENQELRAAVSQQGEQLQTERERGRTAAEDNVRLTCLVAELQKQWEVTQATQNTVKELQTCL 319
Cdd:TIGR02168  221 ELRELELAllvLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRL 300

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   320 QGLELGAAEKEEDYHTALRRLESMLQPLAQELEATRDSLDKKNQHLASFPGWLAMAQQKADTASDTKGRQEPIPSDAAQE 399
Cdd:TIGR02168  301 EQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQ 380

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   400 MQELGEKLQALERERTKVEEVNRQQSAQLEQLVKELQ-LKEDARASLERLVK-EMAPLQEELSGKGQEADQLWRRLQELL 477
Cdd:TIGR02168  381 LETLRSKVAQLELQIASLNNEIERLEARLERLEDRRErLQQEIEELLKKLEEaELKELQAELEELEEELEELQEELERLE 460

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   478 AHTSSweeeLAELRREKKQQQEEKELLEQEVRSLTRQLQFLETQLAQVSQHVSDLEEQKKQLIQDKDHLSQQVGMLER-- 555
Cdd:TIGR02168  461 EALEE----LREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGye 536

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   556 ----LAGPPGPELPVAGEKNEALVPVNSSLQEAWGK------PEEEQRGLQEAQLDDTKVQEGSQE--EELRQANRELEK 623
Cdd:TIGR02168  537 aaieAALGGRLQAVVVENLNAAKKAIAFLKQNELGRvtflplDSIKGTEIQGNDREILKNIEGFLGvaKDLVKFDPKLRK 616

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   624 ELQNVVGRNQLLEGKLQALQadyqalQQRESAIQGSLASLEAEQASIRHL----GDQMEASLLA-------VRKAKEAMK 692
Cdd:TIGR02168  617 ALSYLLGGVLVVDDLDNALE------LAKKLRPGYRIVTLDGDLVRPGGVitggSAKTNSSILErrreieeLEEKIEELE 690

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   693 AQMAEKEAILQSKEGECQQLREEVEQCQQLAEARHRELRALESQCQQQTQLIEVLTAEKGQQgvgpptDNEARELAAQLA 772
Cdd:TIGR02168  691 EKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQL------SKELTELEAEIE 764

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   773 LSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAVLREHKTLVQQLkeqnealnrahvQELLQCSERE 852
Cdd:TIGR02168  765 ELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANL------------RERLESLERR 832

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   853 GALQEERADEAQQREEELRALQEELSqakcsseeaqLEHAELQEQLhrantdtAELGIQVCALTVEKERVEEALAcavqE 932
Cdd:TIGR02168  833 IAATERRLEDLEEQIEELSEDIESLA----------AEIEELEELI-------EELESELEALLNERASLEEALA----L 891

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   933 LQDAKEAASREREGLERQVAGLQQEKESLQEKLKAakaaagslpgLQAQLAQAEQRAQSLQEAAHQELNTLKFQLSAEIM 1012
Cdd:TIGR02168  892 LRSELEELSEELRELESKRSELRRELEELREKLAQ----------LELRLEGLEVRIDNLQERLSEEYSLTLEEAEALEN 961

                          810       820       830
                   ....*....|....*....|....*....|....*...
gi 157738667  1013 DYQSRLKNAGEECKSLRGQLEEQGRQLQAAEEAVEKLK 1050
Cdd:TIGR02168  962 KIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELK 999
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 402-1144 4.14e-25

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: 114.00  E-value: 4.14e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   402 ELGEKLQALERERTKVEEVnRQQSAQLEQLVKELQLKEdarasLERLVKEMAPLQEELSGKGQEADQLWRRLQELLAHTS 481
Cdd:TIGR02168  197 ELERQLKSLERQAEKAERY-KELKAELRELELALLVLR-----LEELREELEELQEELKEAEEELEELTAELQELEEKLE 270

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   482 SWEEELAELRREKKQQQEEKELLEQEVRSLTRQLQFLETQLAQVSQHVSDLEEQKKQLIQDKDHLSQQVGMLERLAGPPG 561
Cdd:TIGR02168  271 ELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELK 350

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   562 PELPVAGEKNEALVPVNSSLQEAWGKPEEEQRGLQ------EAQLDDTKVQEGSQEEELRQANRELEKELQNVVGRNQ-L 634
Cdd:TIGR02168  351 EELESLEAELEELEAELEELESRLEELEEQLETLRskvaqlELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKkL 430

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   635 LEGKLQALQADYQALQQRESAIQGSLASLEAEQASIRHLGDQMEASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQLRE 714
Cdd:TIGR02168  431 EEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKA 510

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   715 EVEQCQQLA----------EARHRELRALESQCQQQTQLIEVLTAEKGQQGVGPPTDNEARELA---------AQLALSQ 775
Cdd:TIGR02168  511 LLKNQSGLSgilgvlseliSVDEGYEAAIEAALGGRLQAVVVENLNAAKKAIAFLKQNELGRVTflpldsikgTEIQGND 590

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   776 AQLEVHQGEVQRLQAQVVDLQAKMRAALDD-------QDKVQSQLSMAEAvLREHKTLV---------------QQLKEQ 833
Cdd:TIGR02168  591 REILKNIEGFLGVAKDLVKFDPKLRKALSYllggvlvVDDLDNALELAKK-LRPGYRIVtldgdlvrpggvitgGSAKTN 669

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   834 NEALNRAhvQELLQCsEREGALQEERADEAQQR----EEELRALQEELSQAKCSSEEAQLEHAELQEQLHRANTDTAELG 909
Cdd:TIGR02168  670 SSILERR--REIEEL-EEKIEELEEKIAELEKAlaelRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLE 746

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   910 IQVCALTVEKERVE---EALACAVQELQDAKEAASREREGLERQVAGLQQEKESLQEKLKAAKAAAGSLPGLQAQLAQAE 986
Cdd:TIGR02168  747 ERIAQLSKELTELEaeiEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERL 826

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   987 QRAQSLQEAAHQELNTLKFQ---LSAEIMDYQSRLKNAGEECKSLRGQLEEQGRQLQAAEEAVEKLKATQADMGEKLSCT 1063
Cdd:TIGR02168  827 ESLERRIAATERRLEDLEEQieeLSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELREL 906

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  1064 SNHLAECQAAMLRKDKEGAALREDLERTQKELEKATTKIQEYYNKLCQEVtnrERNDQKMLADLDDLNRTKKYLEERLIE 1143
Cdd:TIGR02168  907 ESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEA---EALENKIEDDEEEARRRLKRLENKIKE 983


                   .
gi 157738667  1144 L 1144
Cdd:TIGR02168  984 L 984
FYVE pfam01363
FYVE zinc finger; The FYVE zinc finger is named after four proteins that it has been found in: ...
 1169-1232 4.23e-25

FYVE zinc finger; The FYVE zinc finger is named after four proteins that it has been found in: Fab1, YOTB/ZK632.12, Vac1, and EEA1. The FYVE finger has been shown to bind two Zn++ ions. The FYVE finger has eight potential zinc coordinating cysteine positions. Many members of this family also include two histidines in a motif R+HHC+XCG, where + represents a charged residue and X any residue. We have included members which do not conserve these histidine residues but are clearly related.


Pssm-ID: 426221 [Multi-domain]  Cd Length: 68  Bit Score: 99.76  E-value: 4.23e-25
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157738667  1169 RWLGDTEANHCLDCKREFSWMVRRHHCRICGRIFCYYCCNNYVL---SKHGGKKERCCRACFQKLSE 1232
Cdd:pfam01363    2 VWVPDSSATVCMICSKPFTFFRRRHHCRNCGRVFCSACSSKKISllpELGSNKPVRVCDACYDTLQK 68
FYVE smart00064
Protein present in Fab1, YOTB, Vac1, and EEA1; The FYVE zinc finger is named after four ...
 1169-1231 2.31e-24

Protein present in Fab1, YOTB, Vac1, and EEA1; The FYVE zinc finger is named after four proteins where it was first found: Fab1, YOTB/ZK632.12, Vac1, and EEA1. The FYVE finger has been shown to bind two Zn2+ ions. The FYVE finger has eight potential zinc coordinating cysteine positions. The FYVE finger is structurally related to the PHD finger and the RING finger. Many members of this family also include two histidines in a motif R+HHC+XCG, where + represents a charged residue and X any residue. The FYVE finger functions in the membrane recruitment of cytosolic proteins by binding to phosphatidylinositol 3-phosphate (PI3P), which is prominent on endosomes. The R+HHC+XCG motif is critical for PI3P binding.


Pssm-ID: 214499 [Multi-domain]  Cd Length: 68  Bit Score: 97.50  E-value: 2.31e-24
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157738667   1169 RWLGDTEANHCLDCKREFSWMVRRHHCRICGRIFCYYCCNNYVLSKHGG--KKERCCRACFQKLS 1231
Cdd:smart00064    3 HWIPDEEVSNCMGCGKEFNLTKRRHHCRNCGRIFCSKCSSKKAPLPKLGieRPVRVCDDCYENLN 67
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 589-1099 3.61e-22

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 104.25  E-value: 3.61e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  589 EEEQRGLQEAQLDDTKVQEGSQEEELRQANRELEKELQNVVGRNQLLEGKLQALQADYQALQQRESAIQGSLASLEAEQA 668
Cdd:COG1196   247 ELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELA 326

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  669 SIRHLGDQMEASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEV-EQCQQLAEARHRELRALESQCQQQTQLIEVL 747
Cdd:COG1196   327 ELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELaEAEEELEELAEELLEALRAAAELAAQLEELE 406

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  748 TAEKGQQgvgpptDNEARELAAQLALSQAQLEVHQGEVQRLQAqvvdLQAKMRAALDDQDKVQSQLSMAEAVLREHKTLV 827
Cdd:COG1196   407 EAEEALL------ERLERLEEELEELEEALAELEEEEEEEEEA----LEEAAEEEAELEEEEEALLELLAELLEEAALLE 476

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  828 QQLKEQNEALNRAHVQELLQCSEREGALQEERADEAQQREEELRALQEELSQ-AKCSSEEAQLEHAELQEQLHRANTDTA 906
Cdd:COG1196   477 AALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVlIGVEAAYEAALEAALAAALQNIVVEDD 556

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  907 ELGIQVCALTVEKERVEEALACAVQELQDAKEAASREREGLERQVAGLQQEKESLQEKLKAAKAAAGSLPGLQAQLAQAE 986
Cdd:COG1196   557 EVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAAL 636

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  987 QRAQSLQEAAHQELNTLKFQLSAEIMDYQSRLKNAGEEcKSLRGQLEEQGRQLQAAEEAVEKLKATQADMGEKLSCTSNH 1066
Cdd:COG1196   637 RRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAAL-LEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEE 715

                         490       500       510
                  ....*....|....*....|....*....|...
gi 157738667 1067 LAECQAAMLRKDKEGAALREDLERTQKELEKAT 1099
Cdd:COG1196   716 RLEEELEEEALEEQLEAEREELLEELLEEEELL 748
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 226-963 3.09e-21

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: 101.29  E-value: 3.09e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   226 NEALEGFDEMRLELDQLEVREKQLRERMQQLDRENQELRAAVSQQGEQLQTERERgrtaaedNVRLTCLVAELQKQWEVT 305
Cdd:TIGR02168  235 EELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKE-------LYALANEISRLEQQKQIL 307

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   306 QATQNTVKELQTCLQGLELGAAEKEEDYHTALRRLESMLQPLAQELEATRDSLDKKNQHLASFPGWLAMAQQKADTASDT 385
Cdd:TIGR02168  308 RERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSK 387

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   386 KGRQEPIPSDAAQEMQELGEKLQALERERTKVEEVNRQQSAQLE---------QLVKELQLKEDARASLERLVKEMAPLQ 456
Cdd:TIGR02168  388 VAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEeaelkelqaELEELEEELEELQEELERLEEALEELR 467

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   457 EELSGKGQEADQLWRRLQEL---LAHTSSWEEELAELRREKKQQQEEKELLEQEVRSLTRQLQF-------LETQLAQVS 526
Cdd:TIGR02168  468 EELEEAEQALDAAERELAQLqarLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVdegyeaaIEAALGGRL 547

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   527 QH--VSDLEEQKKQLIQDKDHLSQQVGML---------------ERLAGPPG------------PELPVAGEKNEALVPV 577
Cdd:TIGR02168  548 QAvvVENLNAAKKAIAFLKQNELGRVTFLpldsikgteiqgndrEILKNIEGflgvakdlvkfdPKLRKALSYLLGGVLV 627

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   578 NSSLQEAWGKPEEEQRGLQEAQLDDTKV-----------------QEGSQE--------EELRQANRELEKELQNVVGRN 632
Cdd:TIGR02168  628 VDDLDNALELAKKLRPGYRIVTLDGDLVrpggvitggsaktnssiLERRREieeleekiEELEEKIAELEKALAELRKEL 707

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   633 QLLEGKLQALQADYQALQQRESAIQGSLASLEAEQASIRHLGDQMEASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQL 712
Cdd:TIGR02168  708 EELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEEL 787

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   713 REEVEQCQQLAEARHRELRALESQCQQQTqlIEVLTAEKGQQGVgpptDNEARELAAQLALSQAQLEVHQGEVQRLQAQV 792
Cdd:TIGR02168  788 EAQIEQLKEELKALREALDELRAELTLLN--EEAANLRERLESL----ERRIAATERRLEDLEEQIEELSEDIESLAAEI 861

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   793 VDLQAKMRAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNEALNRaHVQELlqcserEGALQEERADEAQQREEELRA 872
Cdd:TIGR02168  862 EELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELES-KRSEL------RRELEELREKLAQLELRLEGL 934

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   873 LQEELSQAKCSSEEAQLEHAELQEQLHRANTDTAELGIQVCALTVEKERVEEALACAVQELQDAKEaasrEREGLERQVA 952
Cdd:TIGR02168  935 EVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKE----RYDFLTAQKE 1010

                          810
                   ....*....|.
gi 157738667   953 GLQQEKESLQE 963
Cdd:TIGR02168 1011 DLTEAKETLEE 1021
RUN cd17671
RUN domain; RUN domain, named after RPIP8 (Rap2 interacting protein 8), UNC-14 and NESCA (new ...
 14-164 5.21e-20

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: 88.25  E-value: 5.21e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   14 IRDLQDAVTELSKEFQEAGEPITDDSTSLHKFSYKLEYLLQFDQKEKAtLLGNKKDYWDYFCACLAKVKGANDG--IRFV 91
Cdd:cd17671     3 VKELLESFADNGEADDSAALTLTDDDPVVGRLCAALEAILSHGLKPKR-FGGGKVSFWDFLEALEKLLPAPSLKqaIRDI 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157738667   92 KSISELRTSLGKGRAFIRYSLVHQRLADTLQQCFMNTKVTSDWYYARSPFLQPKLSSDIVGQLYELTEVQFDL 164
Cdd:cd17671    82 NSLSNVKTDDGRGRAWIRLALNEKSLESYLAALLSDQSLLRKYYEPWALLRDPEEAELFLSLLVGLSSLDFNL 154
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 400-1102 1.46e-19

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 95.39  E-value: 1.46e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  400 MQELGEKLQALERERTKVEEVnRQQSAQLEQLVKELQLKEDARaslerlvkemapLQEELSGKGQEADQLWRRLQELLAH 479
Cdd:COG1196   195 LGELERQLEPLERQAEKAERY-RELKEELKELEAELLLLKLRE------------LEAELEELEAELEELEAELEELEAE 261

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  480 TSSWEEELAELRREKKQQQEEKELLEQEVRSLTRQLQFLETQLAQVSQHVSDLEEQKKQLIQDKDHLSQQvgmlerlagp 559
Cdd:COG1196   262 LAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEE---------- 331

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  560 pgpelpvAGEKNEALVPVNSSLQEAwgkpeEEQRGLQEAQLDDTKVQEGSQEEELRQANRELEKELQnvvgRNQLLEGKL 639
Cdd:COG1196   332 -------LEELEEELEELEEELEEA-----EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE----ELLEALRAA 395

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  640 QALQADYQALQQRESAIQGSLASLEAEQASIrhlgdqmEASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEVEQC 719
Cdd:COG1196   396 AELAAQLEELEEAEEALLERLERLEEELEEL-------EEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL 468

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  720 QQLAEARHRELRALESQCQQQTQLIEVLTAEKGQQGVGPPTDNEARELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKM 799
Cdd:COG1196   469 LEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAAL 548

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  800 RAALDDQDKVQSQlsmAEAVLREHKtlvqQLKEQNEALNRAHVQELLQCSEREGALQEERADEAQQREEELRALQEELSQ 879
Cdd:COG1196   549 QNIVVEDDEVAAA---AIEYLKAAK----AGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDT 621

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  880 AkcssEEAQLEHAELQEQLHRANTDTAELGIQVCALTVEKERVEEALAcAVQELQDAKEAASREREGLERQVAGLQQEKE 959
Cdd:COG1196   622 L----LGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGG-SRRELLAALLEAEAELEELAERLAEEELELE 696

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  960 SLQEKLKAAKAAagslpgLQAQLAQAEQRAQSLQEAAHQELNTLKFQLSAEIMDYQSRLKNAGEEckslrgqlEEQGRQL 1039
Cdd:COG1196   697 EALLAEEEEERE------LAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEE--------LPEPPDL 762

                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157738667 1040 QAAEEAVEKLKATQADMGeklscTSNHLAECQAAMLRKDKEG-AALREDLERTQKELEKATTKI 1102
Cdd:COG1196   763 EELERELERLEREIEALG-----PVNLLAIEEYEELEERYDFlSEQREDLEEARETLEEAIEEI 821
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 247-861 1.27e-18

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 92.69  E-value: 1.27e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  247 KQLRERMQQLDREnqELRAAVSQQGEQLQTERERGRTAAEDNVRLTCLVAELQKQWEVTQATQNTVKELQTCLQGLELGA 326
Cdd:COG1196   216 RELKEELKELEAE--LLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYEL 293

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  327 AEKEEDYHTALRRLESMLQPLAQELEATRDSLDKKNQHLASfpgwlamAQQKADTASDtkgrqepipsDAAQEMQELGEK 406
Cdd:COG1196   294 LAELARLEQDIARLEERRRELEERLEELEEELAELEEELEE-------LEEELEELEE----------ELEEAEEELEEA 356

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  407 LQALERERTKVEEVNRQQSAQLEQLVKELQLKEDARASLERLVKEMAPLQEELSGKGQEADQLWRRLQELLAHTSSWEEE 486
Cdd:COG1196   357 EAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEE 436

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  487 LAELRREKKQQQEEKELLEQEVRSLTRQLQFLETQLAQVSQHVSDLEEQKKQLIQDKDHLSQqvgMLERLAGPPGPELPV 566
Cdd:COG1196   437 EEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE---AEADYEGFLEGVKAA 513

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  567 AGEKNEALVPVNSSLQEAWGK------PEEEQRGLQEAQLDDTKVQEGSQEEELRQ---------ANRELEKELQNVVGR 631
Cdd:COG1196   514 LLLAGLRGLAGAVAVLIGVEAayeaalEAALAAALQNIVVEDDEVAAAAIEYLKAAkagratflpLDKIRARAALAAALA 593

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  632 NQLLEGKLQALQADYQALQQRESAIQGSLASLEAEQASIRHLGDQMEASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQ 711
Cdd:COG1196   594 RGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAA 673

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  712 LREEVEQCQQLAEARHRELRALESQCQQQTQLIEvltaekgqqgvgpptdnEARELAAQLALSQAQLEVHQGEVQRLQAQ 791
Cdd:COG1196   674 LLEAEAELEELAERLAEEELELEEALLAEEEEER-----------------ELAEAEEERLEEELEEEALEEQLEAEREE 736

                         570       580       590       600       610       620       630
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157738667  792 VVDLQAKMRAALDDQDKVQSQLSMAEAVLREHktlVQQLKEQNEAL---NRAHVQELLQCSEREGALQEERAD 861
Cdd:COG1196   737 LLEELLEEEELLEEEALEELPEPPDLEELERE---LERLEREIEALgpvNLLAIEEYEELEERYDFLSEQRED 806
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 820-1166 2.44e-18

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: 91.66  E-value: 2.44e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   820 LREHKTLVQQLKEQNEALNRAHVQELLQCSEREGALQEERADEAQQREEELRALQEELSQAKCSSEEAQLEHAELQEQLH 899
Cdd:TIGR02168  205 LERQAEKAERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIE 284

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   900 RANTDTAELGIQVCALTVEKERVEEALacavQELQDAKEAASREREGLERQVAGLQQEKESLQEKLKAakaaagslpgLQ 979
Cdd:TIGR02168  285 ELQKELYALANEISRLEQQKQILRERL----ANLERQLEELEAQLEELESKLDELAEELAELEEKLEE----------LK 350

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   980 AQLAQAEQRAQSLqEAAHQELNTLKFQLSAEIMDYQSRLKNAGEECKSLRGQLEEQGRQLQAAEEAVEKLKATQADMGEK 1059
Cdd:TIGR02168  351 EELESLEAELEEL-EAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKK 429

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  1060 LS-----CTSNHLAECQAAMLRKDKEGAALREDLERTQKELEKATTKIQEYYNKLcQEVTNRERNDQKMLADLDDLNRTK 1134
Cdd:TIGR02168  430 LEeaelkELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAEREL-AQLQARLDSLERLQENLEGFSEGV 508

                          330       340       350
                   ....*....|....*....|....*....|..
gi 157738667  1135 KYLEERLIELLRDKDALWQKsdaLEFQQKLSA 1166
Cdd:TIGR02168  509 KALLKNQSGLSGILGVLSEL---ISVDEGYEA 537
FYVE_like_SF cd00065
FYVE domain like superfamily; FYVE domain is a 60-80 residue double zinc finger ...
 1178-1227 7.02e-18

FYVE domain like superfamily; FYVE domain is a 60-80 residue double zinc finger motif-containing module named after the four proteins, Fab1, YOTB, Vac1, and EEA1. The canonical FYVE domains are distinguished from other zinc fingers by three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif, which form a compact phosphatidylinositol 3-phosphate (PtdIns3P, also termed PI3P)-binding site. They are found in many membrane trafficking regulators, including EEA1, Hrs, Vac1p, Vps27p, and FENS-1, which locate to early endosomes, specifically bind PtdIns3P, and play important roles in vesicular traffic and in signal transduction. Some proteins, such as rabphilin-3A and alpha-Rab3-interacting molecules (RIMs), are also involved in membrane trafficking and bind to members of the Rab subfamily of GTP hydrolases. However, they contain FYVE-related domains that are structurally similar to the canonical FYVE domains but lack the three signature sequences. At this point, they may not bind to phosphoinositides. In addition, this superfamily also contains the third group of proteins, caspase-associated ring proteins CARP1 and CARP2. They do not localize to membranes in the cell and are involved in the negative regulation of apoptosis, specifically targeting two initiator caspases, caspase 8 and caspase 10, which are distinguished from other FYVE-type proteins. Moreover, these proteins have an altered sequence in the basic ligand binding patch and lack the WxxD motif that is conserved only in phosphoinositide binding FYVE domains. Thus they constitute a family of unique FYVE-type domains called FYVE-like domains. The FYVE domain is structurally similar to the RING domain and the PHD finger. This superfamily also includes ADDz zinc finger domain, which is a PHD-like zinc finger motif that contains two parts, a C2-C2 and a PHD-like zinc finger.


Pssm-ID: 277249 [Multi-domain]  Cd Length: 52  Bit Score: 78.73  E-value: 7.02e-18
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 157738667 1178 HCLDCKREFSWMVRRHHCRICGRIFCYYCCNNYVLSKH--GGKKERCCRACF 1227
Cdd:cd00065     1 RCMLCGKKFSLFRRRHHCRRCGRVFCSKCSSKKLPLPSfgSGKPVRVCDSCY 52
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 284-961 1.16e-17

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 89.23  E-value: 1.16e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  284 AAEDN-VRLTCLVAELQKQWEV--TQATQ-NTVKELQTCLQGLELGAAEKE-EDYHTALRRLESMLQPLAQELEATRDSL 358
Cdd:COG1196   183 ATEENlERLEDILGELERQLEPleRQAEKaERYRELKEELKELEAELLLLKlRELEAELEELEAELEELEAELEELEAEL 262

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  359 DKKNQHLASfpgwLAMAQQKADTASDTKGrqepipsdaaQEMQELGEKLQALERERTKVEEVNRQQSAQLEQLVKELQL- 437
Cdd:COG1196   263 AELEAELEE----LRLELEELELELEEAQ----------AEEYELLAELARLEQDIARLEERRRELEERLEELEEELAEl 328

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  438 ---KEDARASLERLVKEMAPLQEELSGKGQEADQLWRRLQELLAHTSSWEEELAelrrekkqqqeekelleqevrSLTRQ 514
Cdd:COG1196   329 eeeLEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE---------------------ELAEE 387

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  515 LQFLETQLAQVSQHVSDLEEQKKQLIQDKDHLsqqvgmlerlagppgpelpvageknealvpvnsslqeawgkpEEEQRG 594
Cdd:COG1196   388 LLEALRAAAELAAQLEELEEAEEALLERLERL------------------------------------------EEELEE 425

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  595 LQEAQLddtkvQEGSQEEELRQANRELEKELQNVVGRNQLLEGKLQALQADYQALQQRESAIQGSLASLEAEQASIRHLG 674
Cdd:COG1196   426 LEEALA-----ELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAE 500

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  675 DQMEASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEVEQCQQLAEARHRELRALEsqcqqqtQLIEVLTAEKGQQ 754
Cdd:COG1196   501 ADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAA-------AAIEYLKAAKAGR 573

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  755 GVGPPTDNEARELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQN 834
Cdd:COG1196   574 ATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEG 653

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  835 EALNRAHVQELLQCSEREGALQEERADEAQQREEELRALQEELSQAKcSSEEAQLEHAELQEQLHRANTDTAELGIQVCA 914
Cdd:COG1196   654 EGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALL-AEEEEERELAEAEEERLEEELEEEALEEQLEA 732

                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....*..
gi 157738667  915 LTVEKERVEEALACAVQELQDAKEAASREREGLERQVAGLQQEKESL 961
Cdd:COG1196   733 EREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAL 779
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 689-1061 2.26e-17

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 88.46  E-value: 2.26e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  689 EAMKAQMAEKEAILQSKEGECQQLREEVEQcqqlAEaRHRELRALESQCQQQTQLIEVLTAEKgqqgvgpptdnEARELA 768
Cdd:COG1196   182 EATEENLERLEDILGELERQLEPLERQAEK----AE-RYRELKEELKELEAELLLLKLRELEA-----------ELEELE 245

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  769 AQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAvlrEHKTLVQQLKEQNEALNRAHVQEllqc 848
Cdd:COG1196   246 AELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA---ELARLEQDIARLEERRRELEERL---- 318

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  849 sEREGALQEERADEAQQREEELRALQEELSQAKCSSEEAQLEHAELQEQLHRANTDTAelgiqvcaltvEKERVEEALAC 928
Cdd:COG1196   319 -EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA-----------EAEEELEELAE 386

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  929 AVQELQDAKEAASREREGLERQVAGLQQEKESLQEKLKAakaaagslpgLQAQLAQAEQRAQSLQEAAHQELNTLKfQLS 1008
Cdd:COG1196   387 ELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE----------LEEALAELEEEEEEEEEALEEAAEEEA-ELE 455

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 157738667 1009 AEIMDYQSRLKNAGEECKSLRGQLEEQGRQLQAAEEAVEKLKATQADMGEKLS 1061
Cdd:COG1196   456 EEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLE 508
FYVE_PIKfyve_Fab1 cd15725
FYVE domain found in metazoan PIKfyve, fungal and plant Fab1, and similar proteins; PIKfyve, ...
 1170-1228 2.96e-17

FYVE domain found in metazoan PIKfyve, fungal and plant Fab1, and similar proteins; PIKfyve, also termed FYVE finger-containing phosphoinositide kinase, or 1-phosphatidylinositol 3-phosphate 5-kinase, or phosphatidylinositol 3-phosphate 5-kinase (PIP5K3), or phosphatidylinositol 3-phosphate 5-kinase type III (PIPkin-III or type III PIP kinase), is a phosphoinositide 5-kinase that forms a complex with its regulators, the scaffolding protein Vac14 and the lipid phosphatase Fig4. The complex is responsible for synthesizing phosphatidylinositol 3,5-bisphosphate [PtdIns(3,5)P2] from phosphatidylinositol 3-phosphate (PtdIns3P or PI3P). Then phosphatidylinositol-5-phosphate (PtdIns5P) is generated directly from PtdIns(3,5)P2. PtdIns(3,5)P2 and PtdIns5P regulate endosomal trafficking and responses to extracellular stimuli. At this point, PIKfyve is vital in early embryonic development. Moreover, PIKfyve forms a complex with ArPIKfyve (associated regulator of PIKfyve) and SAC3 at the endomembranes, which plays a role in receptor tyrosine kinase (RTK) degradation. The phosphorylation of PIKfyve by AKT can facilitate Epidermal growth factor receptor (EGFR) degradation. In addition, PIKfyve may participate in the regulation of the glutamate transporters EAAT2, EAAT3 and EAAT4, and the cystic fibrosis transmembrane conductance regulator (CFTR). It is also essential for systemic glucose homeostasis and insulin-regulated glucose uptake/GLUT4 translocation in skeletal muscle. It can be activated by protein kinase B (PKB/Akt) and further up-regulates human ether-a-go-go (hERG) channels. This family also includes the yeast and plant orthologs of human PIKfyve, Fab1. PIKfyve and its orthologs share a similar architecture. They contain an N-terminal FYVE domain, a middle region related to the CCT/TCP-1/Cpn60 chaperonins that are involved in productive folding of actin and tubulin, a second middle domain that contains a number of conserved cysteine residues (CCR) unique to this family, and a C-terminal lipid kinase domain related to PtdInsP kinases.


Pssm-ID: 277264 [Multi-domain]  Cd Length: 62  Bit Score: 76.98  E-value: 2.96e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157738667 1170 WLGDTEANHCLDCKREFSWMVRRHHCRICGRIFCYYCCNNYVLSKHGGKKE--RCCRACFQ 1228
Cdd:cd15725     2 WMPDSSCKECYECSEKFTTFRRRHHCRLCGQIFCSRCCNQEIPGKFIGYPGdlRVCTYCCK 62
FYVE_EEA1 cd15730
FYVE domain found in early endosome antigen 1 (EEA1) and similar proteins; EEA1, also termed ...
 1169-1227 4.62e-17

FYVE domain found in early endosome antigen 1 (EEA1) and similar proteins; EEA1, also termed endosome-associated protein p162, or zinc finger FYVE domain-containing protein 2, is an essential component of the endosomal fusion machinery and required for the fusion and maturation of early endosomes in endocytosis. It forms a parallel coiled-coil homodimer in cells. EEA1 serves as the p97 ATPase substrate and the p97 ATPase may regulate the size of early endosomes by governing the oligomeric state of EEA1. It can interact with the GTP-bound form of Rab22a and be involved in endosomal membrane trafficking. EEA1 also functions as an obligate scaffold for angiotensin II-induced Akt activation in early endosomes. It can be phosphorylated by p38 mitogen-activated protein kinase (MAPK) and further regulate mu opioid receptor endocytosis. EEA1 consists of an N-terminal C2H2 Zn2+ finger, four long heptad repeats, and a C-terminal region containing a calmodulin binding (IQ) motif, a Rab5 interaction site, and a FYVE domain. This model corresponds to the FYVE domain that is responsible for binding phosphatidyl inositol-3-phosphate (PtdIns3P or PI3P) on the membrane.


Pssm-ID: 277269 [Multi-domain]  Cd Length: 63  Bit Score: 76.67  E-value: 4.62e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 157738667 1169 RWLGDTEANHCLDCKREFSWMVRRHHCRICGRIFCYYCCNNYVLSKHGGKKERCCRACF 1227
Cdd:cd15730     2 KWADDEEVQNCMACGKGFSVTVRKHHCRQCGNIFCNECSSKTATTPSSKKPVRVCDACF 60
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 821-1140 6.59e-17

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 86.91  E-value: 6.59e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  821 REHKTLVQQLKEQNEALNRAHVQELLQCSEREGALQEERADEAQQREEELRALQEELSQAKCSSEEAQLEHAELQEQLHR 900
Cdd:COG1196   213 ERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYE 292

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  901 ANTDTAELGIQvcaLTVEKERVEEALAcAVQELQDAKEAASREREGLERQVAGLQQEKESLQEKLKAakaaagslpgLQA 980
Cdd:COG1196   293 LLAELARLEQD---IARLEERRRELEE-RLEELEEELAELEEELEELEEELEELEEELEEAEEELEE----------AEA 358

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  981 QLAQAEQRAQSLQEAAHQELNTLKfQLSAEIMDYQSRLKNAGEECKSLRGQLEEQGRQLQAAEEAVEKLKATQADMGEKL 1060
Cdd:COG1196   359 ELAEAEEALLEAEAELAEAEEELE-ELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEE 437

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667 1061 SCTSNHLAECQAAMLRKDKEGAALREDLERTQKELEKATTKIQEYYNKLcQEVTNRERNDQKMLADLDDLNRTKKYLEER 1140
Cdd:COG1196   438 EEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEEL-AEAAARLLLLLEAEADYEGFLEGVKAALLL 516
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 402-1141 4.32e-16

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: 84.35  E-value: 4.32e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   402 ELGEKLQALERERTKVEEVNRQQSAQLEQLVKELQL-KEDARASLERLVKEMAPLQEELSGKGQEADQLWRRLQELLAht 480
Cdd:TIGR02169  195 EKRQQLERLRREREKAERYQALLKEKREYEGYELLKeKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQ-- 272

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   481 ssweEELAELRREKKQQQEEKELLEQEVRSLTRQLQFLETQLAQVSQHVSDLEEQKKQLI-------QDKDHLSQQVGML 553
Cdd:TIGR02169  273 ----LLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEaeidkllAEIEELEREIEEE 348

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   554 ERLAGPPGPELPVAGEKNEALV----PVNSSLQEAWGKPEEEQRGLQEAQ------------LDDTKVQEGSQEEELRQA 617
Cdd:TIGR02169  349 RKRRDKLTEEYAELKEELEDLRaeleEVDKEFAETRDELKDYREKLEKLKreinelkreldrLQEELQRLSEELADLNAA 428

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   618 -------NRELEKELQNVVGRNQLLEGKLQALQADYQALQQRESAIQGSLASLEAEQASIRHLGDQMEASLLAVRKAKEA 690
Cdd:TIGR02169  429 iagieakINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRG 508

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   691 MKAQMAEKEAILQSKEGecqqlreeveQCQQLAEARHRELRALESQCQQQTQLIEVLTAEKGQQGV--------GPPTDN 762
Cdd:TIGR02169  509 GRAVEEVLKASIQGVHG----------TVAQLGSVGERYATAIEVAAGNRLNNVVVEDDAVAKEAIellkrrkaGRATFL 578

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   763 EARELAAQLALSQAqleVHQGEVQRLQAQVVDLQAKMRAA----LDDQDKVQSqLSMAEAVLREHK--TLVQQLKEQNEA 836
Cdd:TIGR02169  579 PLNKMRDERRDLSI---LSEDGVIGFAVDLVEFDPKYEPAfkyvFGDTLVVED-IEAARRLMGKYRmvTLEGELFEKSGA 654

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   837 LNRAHVQ-------------ELLQCSEREGALQEERADEAQQREE---ELRALQEELSQAKCSSEEAQLEHAELQEQLHR 900
Cdd:TIGR02169  655 MTGGSRAprggilfsrsepaELQRLRERLEGLKRELSSLQSELRRienRLDELSQELSDASRKIGEIEKEIEQLEQEEEK 734

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   901 ANTDTAELGIQVCALTVEKERVEEALACAVQELQDAKEAASREREGLERQVAGLQQEK-ESLQEKLKAAKAAAGSLPGLQ 979
Cdd:TIGR02169  735 LKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRiPEIQAELSKLEEEVSRIEARL 814

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   980 AQLAQAEQRAQSLQEAAHQELNTLKfqlsAEIMDYQSRLKNAGEECKSLRGQLEEQGRQLQAAEEAVEKLKATQADMGEK 1059
Cdd:TIGR02169  815 REIEQKLNRLTLEKEYLEKEIQELQ----EQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKE 890

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  1060 LSCTSNHLAECQaamlRKDKEGAALREDLERTQKELeKATTKIQEYYNKLCQEVTNRERNDQKMLADLDDLNRTKKYLEE 1139
Cdd:TIGR02169  891 RDELEAQLRELE----RKIEELEAQIEKKRKRLSEL-KAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEE 965


                   ..
gi 157738667  1140 RL 1141
Cdd:TIGR02169  966 EI 967
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 596-1151 4.94e-16

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: 84.34  E-value: 4.94e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   596 QEAQLDDTKVQEGSQEEELRQANREL---EKELQNVVGRNQLLEGKLQALQADYQALQQRESAIQGSLASLEAEQASIRH 672
Cdd:TIGR02168  237 LREELEELQEELKEAEEELEELTAELqelEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLER 316

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   673 LGDQMEASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEVEQCQQLAEARHR------------------------ 728
Cdd:TIGR02168  317 QLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESrleeleeqletlrskvaqlelqia 396

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   729 ----ELRALESQCQQQTQLIEVLTAEKGQQGvGPPTDNEARELAAQLALS-------QAQLEVHQGEVQRLQAQVVDLQA 797
Cdd:TIGR02168  397 slnnEIERLEARLERLEDRRERLQQEIEELL-KKLEEAELKELQAELEELeeeleelQEELERLEEALEELREELEEAEQ 475

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   798 KMRAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNEALNRAH-----VQELLQCSER-----EGALQE---------- 857
Cdd:TIGR02168  476 ALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSgilgvLSELISVDEGyeaaiEAALGGrlqavvvenl 555

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   858 ERADEAQQ------------------REEELRALQEELSQAKCSSEEAQLEHAELQEQLHRA------------NTDTA- 906
Cdd:TIGR02168  556 NAAKKAIAflkqnelgrvtflpldsiKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKAlsyllggvlvvdDLDNAl 635

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   907 ELGIQ---------------------------VCALTVEKERVEEALACAVQELQDAKEAASREREGLERQVAGLQQEKE 959
Cdd:TIGR02168  636 ELAKKlrpgyrivtldgdlvrpggvitggsakTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELE 715

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   960 SLQEKLKAAKAAagsLPGLQAQLAQAEQRAQSLQEAAHQELNTLKfQLSAEIMDYQSRLKNAGE---ECKSLRGQLEEQ- 1035
Cdd:TIGR02168  716 QLRKELEELSRQ---ISALRKDLARLEAEVEQLEERIAQLSKELT-ELEAEIEELEERLEEAEEelaEAEAEIEELEAQi 791

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  1036 ----------GRQLQAAEEAVEKLKATQADMGEKLSCTSNHLAECQAAMLRKDKEGAALREDLERTQKELEKATT---KI 1102
Cdd:TIGR02168  792 eqlkeelkalREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEElieEL 871

                          650       660       670       680
                   ....*....|....*....|....*....|....*....|....*....
gi 157738667  1103 QEYYNKLCQEVTNRERNDQKMLADLDDLNRTKKYLEERLIELLRDKDAL 1151
Cdd:TIGR02168  872 ESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEEL 920
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 393-1123 9.86e-16

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 83.09  E-value: 9.86e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   393 PSDAAQEMQELgEKLQALERERTKVEEVNRQQSAQLEQLVKELQLKED--------ARASLERLVKEMAPLQEELSGKGQ 464
Cdd:TIGR00618  162 SKEKKELLMNL-FPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLctpcmpdtYHERKQVLEKELKHLREALQQTQQ 240

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   465 EADQLwRRLQELLAHTSSWEEELAELRREKKQQQEEKELLEQEVRSLTRQLQFLetQLAQVSQHVSDLEEQKKQLIQDkd 544
Cdd:TIGR00618  241 SHAYL-TQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAA--PLAAHIKAVTQIEQQAQRIHTE-- 315

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   545 hLSQQVGMLERLAGPPGPELpvageKNEALVPVNSSLQEAWGKPEEEQRGLQEAQLD--DTKVQEGSQEEELRQANRELE 622
Cdd:TIGR00618  316 -LQSKMRSRAKLLMKRAAHV-----KQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSirEISCQQHTLTQHIHTLQQQKT 389

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   623 KELQNVVGRNQLLEgKLQALQADYQALQQRESAIQGSLASLEAEQASIRHLGDQMEASL---LAVRKAKEAMKAQMAEKE 699
Cdd:TIGR00618  390 TLTQKLQSLCKELD-ILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAItctAQCEKLEKIHLQESAQSL 468

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   700 AILQSKEGECQQLREEVEQCQQLAEARHRELRalESQCQQQTQLIEvLTAEKGQQGVGPPTDNEARELAAQLALSQAQLE 779
Cdd:TIGR00618  469 KEREQQLQTKEQIHLQETRKKAVVLARLLELQ--EEPCPLCGSCIH-PNPARQDIDNPGPLTRRMQRGEQTYAQLETSEE 545

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   780 VHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNEALNRAHVQELLQCSEREGALQEER 859
Cdd:TIGR00618  546 DVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQ 625

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   860 ADeaQQREEELRALQEELSQAKCSSEEAQLEHAELQEQLHRAntdtaelgiqvcALTVEKERVEEALACAVQELQDAKEA 939
Cdd:TIGR00618  626 DL--QDVRLHLQQCSQELALKLTALHALQLTLTQERVREHAL------------SIRVLPKELLASRQLALQKMQSEKEQ 691

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   940 ASREREGLERQVAGLQQEKESLQEKLKAAKAAAGSLPGLQAQLAQAEQ-RAQSLQEAAHQELNTLKFQLSAEIMDYQSRL 1018
Cdd:TIGR00618  692 LTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDaLNQSLKELMHQARTVLKARTEAHFNNNEEVT 771

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  1019 --KNAGEECKSLRGQLEEQGRQLqaaEEAVEKLKATQADMGEKLsctsnhlaecQAAMLRKDKEGAALREDLERTQKELE 1096
Cdd:TIGR00618  772 aaLQTGAELSHLAAEIQFFNRLR---EEDTHLLKTLEAEIGQEI----------PSDEDILNLQCETLVQEEEQFLSRLE 838

                          730       740
                   ....*....|....*....|....*..
gi 157738667  1097 KATTKIQEYYNKLCQEVTNRERNDQKM 1123
Cdd:TIGR00618  839 EKSATLGEITHQLLKYEECSKQLAQLT 865
FYVE_LST2 cd15731
FYVE domain found in lateral signaling target protein 2 homolog (Lst2) and similar proteins; ...
 1169-1227 1.61e-15

FYVE domain found in lateral signaling target protein 2 homolog (Lst2) and similar proteins; Lst2, also termed zinc finger FYVE domain-containing protein 28, is a monoubiquitinylated phosphoprotein that functions as a negative regulator of epidermal growth factor receptor (EGFR) signaling. Unlike other FYVE domain-containing proteins, Lst2 displays primarily non-endosomal localization. Its endosomal localization is regulated by monoubiquitinylation. Lst2 physically binds Trim3, also known as BERP or RNF22, which is a coordinator of endosomal trafficking and interacts with Hrs and a complex that biases cargo recycling.


Pssm-ID: 277270 [Multi-domain]  Cd Length: 65  Bit Score: 72.38  E-value: 1.61e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157738667 1169 RWLGDTEANHCLDCKREFSWMVRRHHCRICGRIFCYYC-CNNYVLSKHG-GKKERCCRACF 1227
Cdd:cd15731     4 LWVPDEACPQCMACSAPFTVLRRRHHCRNCGKIFCSRCsSNSVPLPRYGqMKPVRVCNHCF 64
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
567-1024 1.09e-14

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 79.57  E-value: 1.09e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  567 AGEKNEALVPV---NSSLQEAWgkpeeEQRGLQEAQLDDTKVQEGSQE-EELRQANRELEKELQNVVGRNQLLEGKLQAL 642
Cdd:COG4913   247 AREQIELLEPIrelAERYAAAR-----ERLAELEYLRAALRLWFAQRRlELLEAELEELRAELARLEAELERLEARLDAL 321

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  643 QADYQALQQRESAIQGS-LASLEAEQASIRHLGDQMEASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEVEQCQQ 721
Cdd:COG4913   322 REELDELEAQIRGNGGDrLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELE 401

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  722 LAEARHRELRALESQCQQQ-TQLIEVLTAEKGQQGVGPPTDNEAR-ELAAQLALSQAQL-------EVHQGEV------- 785
Cdd:COG4913   402 ALEEALAEAEAALRDLRRElRELEAEIASLERRKSNIPARLLALRdALAEALGLDEAELpfvgeliEVRPEEErwrgaie 481

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  786 -------------QRLQAQVVDL--QAKMRAALDDQdKVQSQLSMAEAVLREHKTLVQQLK-EQNEAlnRAHVQELLQ-- 847
Cdd:COG4913   482 rvlggfaltllvpPEHYAAALRWvnRLHLRGRLVYE-RVRTGLPDPERPRLDPDSLAGKLDfKPHPF--RAWLEAELGrr 558

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  848 ----CSEREGALQEER----------------------------------ADEAQQREEELRALQEELSQAKCSSEEAQL 889
Cdd:COG4913   559 fdyvCVDSPEELRRHPraitragqvkgngtrhekddrrrirsryvlgfdnRAKLAALEAELAELEEELAEAEERLEALEA 638

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  890 EHAELQEQLHRANT---------DTAELGIQVCALTVEKERVE------EALACAVQELQDAKEAASREREGLERQVAGL 954
Cdd:COG4913   639 ELDALQERREALQRlaeyswdeiDVASAEREIAELEAELERLDassddlAALEEQLEELEAELEELEEELDELKGEIGRL 718

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157738667  955 QQEKESLQEKLKAAKAAAGSLPGLQAQLAQA---EQRAQSLQEAAHQElntLKFQLSAEIMDYQSRLKNAGEE 1024
Cdd:COG4913   719 EKELEQAEEELDELQDRLEAAEDLARLELRAlleERFAAALGDAVERE---LRENLEERIDALRARLNRAEEE 788
FYVE_endofin cd15729
FYVE domain found in endofin and similar proteins; Endofin, also termed zinc finger FYVE ...
 1170-1230 1.10e-14

FYVE domain found in endofin and similar proteins; Endofin, also termed zinc finger FYVE domain-containing protein 16 (ZFY16), or endosome-associated FYVE domain protein, is a FYVE domain-containing protein that is localized to EEA1-containing endosomes. It is regulated by phosphoinositol lipid and engaged in endosome-mediated receptor modulation. Endofin is involved in Bone morphogenetic protein (BMP) signaling through interacting with Smad1 preferentially and enhancing Smad1 phosphorylation and nuclear localization upon BMP stimulation. It also functions as a scaffold protein that brings Smad4 to the proximity of the receptor complex in Transforming growth factor (TGF)-beta signaling. Moreover, endofin is a novel tyrosine phosphorylation target downstream of epidermal growth factor receptor (EGFR) in EGF-signaling. In addition, endofin plays a role in endosomal trafficking by recruiting cytosolic TOM1, an important molecule for membrane recruitment of clathrin, onto endosomal membranes.


Pssm-ID: 277268 [Multi-domain]  Cd Length: 68  Bit Score: 70.07  E-value: 1.10e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157738667 1170 WLGDTEANHCLDCKREFSWMVRRHHCRICGRIFCYYCCN-NYVLSKHGGKKERCCRACFQKL 1230
Cdd:cd15729     7 WVPDSEAPNCMQCEVKFTFTKRRHHCRACGKVLCSACCSlKARLEYLDNKEARVCVPCYQTL 68
FYVE_RUFY1_like cd15721
FYVE domain found in RUN and FYVE domain-containing protein RUFY1, RUFY2 and similar proteins; ...
 1170-1227 3.62e-14

FYVE domain found in RUN and FYVE domain-containing protein RUFY1, RUFY2 and similar proteins; This family includes RUN and FYVE domain-containing protein RUFY1 and RUFY2. RUFY1, also termed 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 homologue 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 termed 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. Both RUFY1 and RUFY2 contain an N-terminal RUN domain and a C-terminal FYVE domain with two coiled-coil domains in-between.


Pssm-ID: 277261 [Multi-domain]  Cd Length: 58  Bit Score: 68.18  E-value: 3.62e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 157738667 1170 WLGDTEANHCLDCKREFSWMVRRHHCRICGRIFCYYCCNNYVLSKHGGKKERCCRACF 1227
Cdd:cd15721     1 WADDKEVTHCQQCEKEFSLSRRKHHCRNCGGIFCNSCSDNTMPLPSSAKPVRVCDTCY 58
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 228-1145 3.75e-14

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: 78.19  E-value: 3.75e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   228 ALEGFDEMRLELDQLEVREKQLRERMQQLdrenqelraavsqQGEQLQTERERGRTAAEDNVRLTCLVAELQKQWEVTQA 307
Cdd:TIGR02169  175 ALEELEEVEENIERLDLIIDEKRQQLERL-------------RREREKAERYQALLKEKREYEGYELLKEKEALERQKEA 241

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   308 TQNTVKELQTCLQGLELGAAEKEEDYHTALRRLESMLQPLAQELEATRDSLDKKnqhLASFPGWLAMAQQKADtasdtkg 387
Cdd:TIGR02169  242 IERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEK---IGELEAEIASLERSIA------- 311

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   388 rqepipsDAAQEMQELGEKLQALERERTKVEEvnrqqsaQLEQLVKELqlkedaraslERLVKEMAPLQEELSGKGQEAD 467
Cdd:TIGR02169  312 -------EKERELEDAEERLAKLEAEIDKLLA-------EIEELEREI----------EEERKRRDKLTEEYAELKEELE 367

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   468 QLWRRLQELLAHTSSWEeelaelrREKKQQQEEKELLEQEVRSLTRQ-------LQFLETQLAQVSQHVSDLEEQKKQLI 540
Cdd:TIGR02169  368 DLRAELEEVDKEFAETR-------DELKDYREKLEKLKREINELKREldrlqeeLQRLSEELADLNAAIAGIEAKINELE 440

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   541 QDKDHLSQQVGMLERlagppgpELPVAGEKNEALVPVNSSLQEAWGKPEEEQRGLQE--AQLDDTKVQEGSQEEELRQAN 618
Cdd:TIGR02169  441 EEKEDKALEIKKQEW-------KLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRelAEAEAQARASEERVRGGRAVE 513

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   619 RELEKELQNVVGrnqlLEGKLQALQADYQAlqQRESAIQGSLASLEAE-----QASIRHLGDQM--EASLLAVRKakeaM 691
Cdd:TIGR02169  514 EVLKASIQGVHG----TVAQLGSVGERYAT--AIEVAAGNRLNNVVVEddavaKEAIELLKRRKagRATFLPLNK----M 583

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   692 KAQMAEKEAIlqSKEGECQQLREEVEQCQQLAEA------------RHRELRALESQCQQQTQLIEVL----------TA 749
Cdd:TIGR02169  584 RDERRDLSIL--SEDGVIGFAVDLVEFDPKYEPAfkyvfgdtlvveDIEAARRLMGKYRMVTLEGELFeksgamtggsRA 661

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   750 EKGQQGVGPPTDNEARELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEavlREHKTLVQQ 829
Cdd:TIGR02169  662 PRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLE---QEEEKLKER 738

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   830 LKEQnealnRAHVQELLQCSEREGALQEERADEAQQREEELRALQEELsqakcSSEEAQLEHAELQeqlhrantdtaELG 909
Cdd:TIGR02169  739 LEEL-----EEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEAL-----NDLEARLSHSRIP-----------EIQ 797

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   910 IQVCALTVEKERVEEALACAVQELQD---AKEAASREREGLERQVAGLQQEKESLQEKLKAakaaagslpgLQAQLAQAE 986
Cdd:TIGR02169  798 AELSKLEEEVSRIEARLREIEQKLNRltlEKEYLEKEIQELQEQRIDLKEQIKSIEKEIEN----------LNGKKEELE 867

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   987 QRAQSLQeaahqelntlkfqlsAEIMDYQSRLKNAGEECKSLRGQLEEQGRQLQAAEEAVEKLKATQADMGEKLSCTSNH 1066
Cdd:TIGR02169  868 EELEELE---------------AALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEE 932

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  1067 LAECQAAmLRKDKEGAALREDLERTQKELEKATTKIQEYynklcQEVTNRERND-QKMLADLDDLNRTKKYLEERLIELL 1145
Cdd:TIGR02169  933 LSEIEDP-KGEDEEIPEEELSLEDVQAELQRVEEEIRAL-----EPVNMLAIQEyEEVLKRLDELKEKRAKLEEERKAIL 1006
FYVE_MTMR3 cd15732
FYVE domain found in myotubularin-related protein 3 (MTMR3) and similar proteins; MTMR3, also ...
 1169-1227 4.73e-14

FYVE domain found in myotubularin-related protein 3 (MTMR3) and similar proteins; MTMR3, also termed Myotubularin-related phosphatase 3, or FYVE domain-containing dual specificity protein phosphatase 1 (FYVE-DSP1), or zinc finger FYVE domain-containing protein 10, is a ubiquitously expressed phosphoinositide 3-phosphatase specific for phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) and phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2) and PIKfyve, which produces PtdIns(3,5)P2 from PtdIns3P. It regulates cell migration through modulating phosphatidylinositol 5-phosphate (PtdIns5P) levels. MTMR3 contains an N-terminal PH-GRAM (PH-G) domain, a MTM phosphatase domain, a coiled-coil region, and a C-terminal FYVE domain. Unlike conventional FYVE domains, the FYVE domain of MTMR3 neither confers endosomal localization nor binds to PtdIns3P. It is also not required for the enzyme activity of MTMR3. In contrast, the PH-G domain binds phosphoinositides.


Pssm-ID: 277271 [Multi-domain]  Cd Length: 61  Bit Score: 68.00  E-value: 4.73e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157738667 1169 RWLGDTEANHCLDCKREFSWMVRRHHCRICGRIFCYYCCNN--YVLSKHGGKKERCCRACF 1227
Cdd:cd15732     1 RWVPDHLAASCYGCEREFWLASRKHHCRNCGNVFCGSCCNQklPVPSQQLFEPSRVCKSCF 61
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 227-779 4.95e-14

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 77.67  E-value: 4.95e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  227 EALEGFDEMRLELDQLEVREKQLRERMQQLDRENQELRAAVSQQGEQLQTERERGRTAAEDNVRLTCLVAELQKQWEVTQ 306
Cdd:COG1196   257 ELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELE 336

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  307 ATQNTVKELQTCLQGLELGAAEKEEDYHTALRRLESMLQPLAQELEATRDSLDKKNQHLASFpgwLAMAQQKADTASDTK 386
Cdd:COG1196   337 EELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL---AAQLEELEEAEEALL 413

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  387 GRQEPIPSDAAQEMQELGEKLQALERERTKVEEVNRQQSAQLEQLVKELQLKEDARASLERLVKEMAPLQEELSGKGQEA 466
Cdd:COG1196   414 ERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARL 493

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  467 DQLWRRLQELLAHTSSWEEELAELRREKKQQQEEKELLEQEVRSLTrqlqfLETQLAQVSQH-VSDLEEQKKQLIQDkdh 545
Cdd:COG1196   494 LLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAA-----LEAALAAALQNiVVEDDEVAAAAIEY--- 565

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  546 lsqqvgmLERLAGPPGPELPVAGEKNEALVPVNSSLQEAWGKPEEEQRGLQEAQLDDTKVQEGSQEEELRQANRElekel 625
Cdd:COG1196   566 -------LKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLE----- 633

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  626 qNVVGRNQLLEGKLQALQADYQALQQRESAIQGSLASLEAEQASIRHLgdQMEASLLAVRKAKEAMKAQMAEKEAILQSK 705
Cdd:COG1196   634 -AALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAE--LEELAERLAEEELELEEALLAEEEEERELA 710

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157738667  706 EGECQQLREEVEQCQQLAEARHRELRALESQCQQQTQLIEVLTAEkgqqgvgPPTDNEARELAAQLALSQAQLE 779
Cdd:COG1196   711 EAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEE-------LPEPPDLEELERELERLEREIE 777
FYVE_MTMR4 cd15733
FYVE domain found in myotubularin-related protein 4 (MTMR4) and similar proteins; MTMR4, also ...
 1170-1227 1.52e-13

FYVE domain found in myotubularin-related protein 4 (MTMR4) and similar proteins; MTMR4, also termed FYVE domain-containing dual specificity protein phosphatase 2 (FYVE-DSP2), or zinc finger FYVE domain-containing protein 11, is an dual specificity protein phosphatase that specifically dephosphorylates phosphatidylinositol 3-phosphate (PtdIns3P or PI3P). It is localizes to early endosomes, as well as to Rab11- and Sec15-positive recycling endosomes, and regulates sorting from early endosomes. Moreover, MTMR4 is preferentially associated with and dephosphorylated the activated regulatory Smad proteins (R-Smads) in cytoplasm to keep transforming growth factor (TGF) beta signaling in homeostasis. It also functions as an essential negative modulator for the homeostasis of bone morphogenetic protein (BMP)/decapentaplegic (Dpp) signaling. In addition, MTMR4 acts as a novel interactor of the ubiquitin ligase Nedd4 (neural-precursor-cell-expressed developmentally down-regulated 4) and may play a role in the biological process of muscle breakdown. MTMR4 contains an N-terminal PH-GRAM (PH-G) domain, a MTM phosphatase domain, a coiled-coil region, and a C-terminal FYVE domain.


Pssm-ID: 277272 [Multi-domain]  Cd Length: 60  Bit Score: 66.69  E-value: 1.52e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157738667 1170 WLGDTEANHCLDCKREFsWMV-RRHHCRICGRIFCYYCCNnyvlSKHGGKKE------RCCRACF 1227
Cdd:cd15733     1 WVPDHAASHCFGCDCEF-WLAkRKHHCRNCGNVFCADCSN----YKLPIPDEqlydpvRVCNSCY 60
FYVE_ZF21 cd15727
FYVE domain found in zinc finger FYVE domain-containing protein 21 (ZF21) and similar proteins; ...
 1167-1212 1.58e-13

FYVE domain found in zinc finger FYVE domain-containing protein 21 (ZF21) and similar proteins; ZF21 is phosphoinositide-binding protein that functions as a regulator of focal adhesions and cell movement through interaction with focal adhesion kinase. It can also bind to the cytoplasmic tail of membrane type 1 matrix metalloproteinase, a potent invasion-promoting protease, and play a key role in regulating multiple aspects of cancer cell migration and invasion. ZF21 contains a FYVE domain, which corresponds to this model.


Pssm-ID: 277266 [Multi-domain]  Cd Length: 64  Bit Score: 66.63  E-value: 1.58e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 157738667 1167 EERWLGDTEANHCLDCKREFSWMVRRHHCRICGRIFCYYCCNNYVL 1212
Cdd:cd15727     1 EPPWVPDKECPVCMSCKKKFDFFKRRHHCRRCGKCFCSDCCSNKVP 46
RUN_RUFY1_like cd17681
RUN domain found in RUN and FYVE domain-containing proteins, RUFY1, RUFY2, RUFY3 and similar ...
 20-135 3.16e-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: 3.16e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   20 AVTELS-KEFQEA----GEPITDDSTSLHKFSYKLEYLLQFDQKEKATLLGNKKDYWDYFCACLAKVKGANDGIRFVKSI 94
Cdd:cd17681     7 NLAKLSiKELIESalsfGRTLDSDHVPLQQFFVILEHVLRHGLKVKKSFLGPNKSFWPVLEHVEKLVPEANEITASVRDL 86

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 157738667   95 SELRTSLGKGRAFIRYSLVHQRLADTLQQCFMNTKVTSDWY 135
Cdd:cd17681    87 PGIKTPLGRARAWLRLALMQKKLADYFRALIENKDLLSEFY 127
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 511-1167 5.44e-13

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: 74.33  E-value: 5.44e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   511 LTRQLQFLETQLAQVSQHVSDLEEQKKQLIQDKDHLSQQVGMLERLagppgpelpvagekneaLVPVNSSLQEawgKPEE 590
Cdd:TIGR02169  228 LLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQL-----------------LEELNKKIKD---LGEE 287

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   591 EQRGLQEaQLDDTKVQEGSQEEELRQANRELEKelqnvvgrnqlLEGKLQALQADYqalqqreSAIQGSLASLEAEQASI 670
Cdd:TIGR02169  288 EQLRVKE-KIGELEAEIASLERSIAEKERELED-----------AEERLAKLEAEI-------DKLLAEIEELEREIEEE 348

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   671 RHLGDQMEASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEVEQCQQLAEARHRELRALESQCQQQTQLIEVLTAE 750
Cdd:TIGR02169  349 RKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAA 428

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   751 -KGQQGVGPPTDNEARELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAVLREHKTLVQQ 829
Cdd:TIGR02169  429 iAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRG 508

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   830 LKEQNEALNR------AHVQELLQCSERE---------GALQ------EERADEAQQREEE----------LRALQEELS 878
Cdd:TIGR02169  509 GRAVEEVLKAsiqgvhGTVAQLGSVGERYataievaagNRLNnvvvedDAVAKEAIELLKRrkagratflpLNKMRDERR 588

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   879 QAKCSSEEAQLEHA----ELQEQLHRA------------NTDTA-ELGIQVCALTVEKERVE-----------EALACAV 930
Cdd:TIGR02169  589 DLSILSEDGVIGFAvdlvEFDPKYEPAfkyvfgdtlvveDIEAArRLMGKYRMVTLEGELFEksgamtggsraPRGGILF 668

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   931 QELQDAKEAASRER-EGLERQVAGLQQEKESLQ----EKLKAAKAAAGSLPGLQAQLAQAEQRAQSLQEAAHqelntlkf 1005
Cdd:TIGR02169  669 SRSEPAELQRLRERlEGLKRELSSLQSELRRIEnrldELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLE-------- 740

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  1006 QLSAEIMDYQSRLKNAGEECKSLRGQLEEQGRQLQAAEEAVEKLKATQADmgEKLSCTSNHLAECQAAMLRKDKEGAALR 1085
Cdd:TIGR02169  741 ELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSH--SRIPEIQAELSKLEEEVSRIEARLREIE 818

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  1086 EDLERTQKELEKATTKIQEYYNK----------LCQEVTNRERNDQKMLADLDDLNRTKKYLEERLIELLRDKDAL-WQK 1154
Cdd:TIGR02169  819 QKLNRLTLEKEYLEKEIQELQEQridlkeqiksIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELeAQL 898

                          730
                   ....*....|...
gi 157738667  1155 SDALEFQQKLSAE 1167
Cdd:TIGR02169  899 RELERKIEELEAQ 911
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 619-1183 6.68e-13

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: 74.00  E-value: 6.68e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   619 RELEKELQNVVGRNQLLEGKLQALQADYQ-----ALQQRESAIQGSLASLEAEQASIRHLGDQMEASLLAVRKAKEAMKA 693
Cdd:pfam15921  227 RELDTEISYLKGRIFPVEDQLEALKSESQnkielLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQE 306

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   694 QMAEKEAI----LQSKEGECQQLREEVEQCQQLAEARHRELRalESQCQQQTQLIEVLTAEKGQQGVGPPTDNEARELAA 769
Cdd:pfam15921  307 QARNQNSMymrqLSDLESTVSQLRSELREAKRMYEDKIEELE--KQLVLANSELTEARTERDQFSQESGNLDDQLQKLLA 384

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   770 -------QLALSQAQ---------------------LEVHQGEVQRLQAQVVDLQAKMRAALDDQdkvQSQLSMAEAVLR 821
Cdd:pfam15921  385 dlhkrekELSLEKEQnkrlwdrdtgnsitidhlrreLDDRNMEVQRLEALLKAMKSECQGQMERQ---MAAIQGKNESLE 461

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   822 EHKTLVQQLKEQNEALnRAHVQEL------LQCSERE-----GALQE-ERADEAQQRE------------EELRALQEE- 876
Cdd:pfam15921  462 KVSSLTAQLESTKEML-RKVVEELtakkmtLESSERTvsdltASLQEkERAIEATNAEitklrsrvdlklQELQHLKNEg 540

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   877 --LSQAKCSSEEAQLEHAE-------LQEQLHRANTDTAELGIQVCALTVEKERVEEALACAVQELQ------DAKEAAS 941
Cdd:pfam15921  541 dhLRNVQTECEALKLQMAEkdkvieiLRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQefkilkDKKDAKI 620

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   942 REregLERQVAGLQQEKESLqeklkaakAAAGSlPGLQAQLAQAEQRAQSLQEA--AHQELNTLkfqlSAEIMDYQSRLK 1019
Cdd:pfam15921  621 RE---LEARVSDLELEKVKL--------VNAGS-ERLRAVKDIKQERDQLLNEVktSRNELNSL----SEDYEVLKRNFR 684

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  1020 NAGEECKSLRGQLEeqgRQLQAAEEAVEKLKATQADMgeklSCTSNHLAECQAAMLRKDKEGAALREDLERTQKELEKAT 1099
Cdd:pfam15921  685 NKSEEMETTTNKLK---MQLKSAQSELEQTRNTLKSM----EGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAM 757

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  1100 TK-------IQEYYNKLCQEVTNRERNDQKMLADLDDLNRTKKYLEERL--IELLRDKDALwQKSDALEFQQKLSAEERW 1170
Cdd:pfam15921  758 TNankekhfLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVanMEVALDKASL-QFAECQDIIQRQEQESVR 836

                          650
                   ....*....|...
gi 157738667  1171 LgdtEANHCLDCK 1183
Cdd:pfam15921  837 L---KLQHTLDVK 846
FYVE_scVPS27p_like cd15760
FYVE domain found in Saccharomyces cerevisiae vacuolar protein sorting-associated protein 27 ...
 1175-1227 8.07e-13

FYVE domain found in Saccharomyces cerevisiae vacuolar protein sorting-associated protein 27 (scVps27p) and similar proteins; scVps27p, also termed Golgi retention defective protein 11, is the putative yeast counterpart of the mammalian protein Hrs and is involved in endosome maturation. It is a mono-ubiquitin-binding protein that interacts with ubiquitinated cargoes, such as Hse1p, and is required for protein sorting into the multivesicular body. Vps27p forms a complex with Hse1p. The complex binds ubiquitin and mediates endosomal protein sorting. At the endosome, Vps27p and a trimeric protein complex, ESCRT-1, bind ubiquitin and are important for multivesicular body (MVB) sorting. Vps27p contains an N-terminal VHS (Vps27/Hrs/STAM) domain, a FYVE domain that binds PtdIns3P, followed by two ubiquitin-interacting motifs (UIMs), and a C-terminal clathrin-binding motif.


Pssm-ID: 277299 [Multi-domain]  Cd Length: 59  Bit Score: 64.63  E-value: 8.07e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 157738667 1175 EANHCLDCKREFSWMVRRHHCRICGRIFCYYCCNNYV-LSKHGGKKERC--CRACF 1227
Cdd:cd15760     4 PDSRCDVCRKKFGLFKRRHHCRNCGDSFCSEHSSRRIpLPHLGPLGVPQrvCDRCF 59
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
395-1019 9.63e-13

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 73.41  E-value: 9.63e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  395 DAAQEMQELgekLQALERERTKVEEVnRQQSAQLEQLVKELQLKEDARASLERLVKEMAPLQeelsgkgqeadqLWRRLQ 474
Cdd:COG4913   225 EAADALVEH---FDDLERAHEALEDA-REQIELLEPIRELAERYAAARERLAELEYLRAALR------------LWFAQR 288

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  475 ELLAhtssWEEELAELRREKKQQQEEKELLEQEVRSLTRQLQFLETQLAQVS-QHVSDLEEQKKQLIQDKDHLSQQVGML 553
Cdd:COG4913   289 RLEL----LEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARL 364

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  554 ERLAGPPGPELPVAGEKNEALVPVNSSLQEAWgkpeEEQRGLQEAQLDDTKVqegsQEEELRQANRELEKELQNVVGRNQ 633
Cdd:COG4913   365 EALLAALGLPLPASAEEFAALRAEAAALLEAL----EEELEALEEALAEAEA----ALRDLRRELRELEAEIASLERRKS 436

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  634 LLEGKLQALQADY-QALQQRES--------------------AIQGSLASL------EAEQAS-----IRHLGDQMEASL 681
Cdd:COG4913   437 NIPARLLALRDALaEALGLDEAelpfvgelievrpeeerwrgAIERVLGGFaltllvPPEHYAaalrwVNRLHLRGRLVY 516

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  682 LAVRKAKEAMKAQMAEKEAI---LQSKEGECQQ-LREEVEQ-----CQQLAEARHRELRALESQCQ--QQTQLievltAE 750
Cdd:COG4913   517 ERVRTGLPDPERPRLDPDSLagkLDFKPHPFRAwLEAELGRrfdyvCVDSPEELRRHPRAITRAGQvkGNGTR-----HE 591

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  751 KGQQGVGPPT-----DNEAR--ELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKmRAALDDQDKVQSQLSMAEAVLREh 823
Cdd:COG4913   592 KDDRRRIRSRyvlgfDNRAKlaALEAELAELEEELAEAEERLEALEAELDALQER-REALQRLAEYSWDEIDVASAERE- 669

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  824 ktlVQQLKEQNEALNRAHvQELLQCSEREGALQEERaDEAQQREEELRALQEELSQAKcssEEAQLEHAELQEQLHRANT 903
Cdd:COG4913   670 ---IAELEAELERLDASS-DDLAALEEQLEELEAEL-EELEEELDELKGEIGRLEKEL---EQAEEELDELQDRLEAAED 741

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  904 DTAELGIQVCALTVEKERVEEALACAVQELQDAKEAASREREGLERQVAGLQQE-KESLQEKLKAAKAAAGSLPGLQAQL 982
Cdd:COG4913   742 LARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAfNREWPAETADLDADLESLPEYLALL 821

                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....*.
gi 157738667  983 AQ--------AEQR-AQSLQEAAHQELNTLKFQLSAEIMDYQSRLK 1019
Cdd:COG4913   822 DRleedglpeYEERfKELLNENSIEFVADLLSKLRRAIREIKERID 867
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 861-1168 9.97e-13

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 73.43  E-value: 9.97e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  861 DEAQQREEELRALQEELSQAKCSSEEAQLEHAELQEQLHRANTDTAELGIQVCALTVEKERVEealacaVQELQDAKEAA 940
Cdd:COG1196   220 EELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELE------LEEAQAEEYEL 293

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  941 SREREGLERQVAGLQQEKESLQEKLkaakaaagslpglqAQLAQAEQRAQSLQEAAHQELNTLKfqlsAEIMDYQSRLKN 1020
Cdd:COG1196   294 LAELARLEQDIARLEERRRELEERL--------------EELEEELAELEEELEELEEELEELE----EELEEAEEELEE 355

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667 1021 AGEECKSLRGQLEEQGRQLQAAEEAVEKLKATQADMGEKLSCTSNHLAECQAAMLRKDKEGAALREDLERTQKELEKATT 1100
Cdd:COG1196   356 AEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEE 435

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157738667 1101 KIQEYYNKLCQEVTNRERNDQKMLADLDDLNRTKKYLEERLIELLRDKDALWQKSDALEFQQKLSAEE 1168
Cdd:COG1196   436 EEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADY 503
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 219-1096 1.10e-12

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: 73.23  E-value: 1.10e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   219 DLNSPLNNEALEGFDEMRLELDQLEVREKQLRERMQQLDRENQELRAAVSQQGEQLQT---ERERGRTAAEDNVRltclv 295
Cdd:pfam15921   60 ELDSPRKIIAYPGKEHIERVLEEYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTklqEMQMERDAMADIRR----- 134

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   296 AELQKQWEVTQATQNTVKELQT--CLQGLELGAAEKE-EDYHTALRRLESMLQPLAQELEATRDSLDKK--------NQH 364
Cdd:pfam15921  135 RESQSQEDLRNQLQNTVHELEAakCLKEDMLEDSNTQiEQLRKMMLSHEGVLQEIRSILVDFEEASGKKiyehdsmsTMH 214

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   365 LASFPGWLAMAQQKADTA-SDTKGRQEPIPsdaaqemqelgEKLQALERE-RTKVEEVNRQQSAQLEQLVKELQLK---- 438
Cdd:pfam15921  215 FRSLGSAISKILRELDTEiSYLKGRIFPVE-----------DQLEALKSEsQNKIELLLQQHQDRIEQLISEHEVEitgl 283

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   439 ----EDARASLERLVKEMAPLQEElsGKGQEADQLwRRLQELLAHTSSWEEELAELRREKKQQQEEKELLEQEVRSltrQ 514
Cdd:pfam15921  284 tekaSSARSQANSIQSQLEIIQEQ--ARNQNSMYM-RQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANS---E 357

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   515 LQFLETQLAQVSQHVSDLEEQKKQLIQDKDHLSQqvgmlerlagppgpELPVAGEKNEALvpvnsslqeaWgkpeeeqrg 594
Cdd:pfam15921  358 LTEARTERDQFSQESGNLDDQLQKLLADLHKREK--------------ELSLEKEQNKRL----------W--------- 404

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   595 lqeaqldDTKVQEGSQEEELRqanRELEKELQNVvgrnQLLEGKLQALQADYQA-LQQRESAIQGSLASLEaeqaSIRHL 673
Cdd:pfam15921  405 -------DRDTGNSITIDHLR---RELDDRNMEV----QRLEALLKAMKSECQGqMERQMAAIQGKNESLE----KVSSL 466

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   674 GDQMEASLLAVRKAKEAMKAqmaeKEAILQSKEGECQQLREEVEQCQQLAEARHRELRALESQCQQQTQLIEVLTAEkGQ 753
Cdd:pfam15921  467 TAQLESTKEMLRKVVEELTA----KKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNE-GD 541

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   754 QGVGPPTDNEARELaaQLALSQAQLEVHQGEVQRLqAQVVDLQAKMRAALD-DQDKVQSQLSMAEAVLREHKTL------ 826
Cdd:pfam15921  542 HLRNVQTECEALKL--QMAEKDKVIEILRQQIENM-TQLVGQHGRTAGAMQvEKAQLEKEINDRRLELQEFKILkdkkda 618

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   827 -VQQLKEQNEALNRAHVQELLQCSEREGALQeeraDEAQQREEELRALQEELSQAKCSSEEAQLEHAELQEQLHRANTDT 905
Cdd:pfam15921  619 kIRELEARVSDLELEKVKLVNAGSERLRAVK----DIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTT 694

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   906 AELGIQVCALTVEKERVEEALacavQELQDAKEAASREREGLERQVAGLQQEKESLQEKLKAakaaagslpgLQAQLAQA 985
Cdd:pfam15921  695 NKLKMQLKSAQSELEQTRNTL----KSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQF----------LEEAMTNA 760

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   986 EQRAQSLQEAahqelntlKFQLSAEimdyqsrLKNAGEECKSLRGQLEeqgrQLQAAEeavEKLKATQADMGEKLSCTSN 1065
Cdd:pfam15921  761 NKEKHFLKEE--------KNKLSQE-------LSTVATEKNKMAGELE----VLRSQE---RRLKEKVANMEVALDKASL 818

                          890       900       910
                   ....*....|....*....|....*....|.
gi 157738667  1066 HLAECQAAMLRKDKEGAALREDLERTQKELE 1096
Cdd:pfam15921  819 QFAECQDIIQRQEQESVRLKLQHTLDVKELQ 849
FYVE_RUFY1 cd15758
FYVE domain found in RUN and FYVE domain-containing protein 1 (RUFY1) and similar proteins; ...
 1170-1226 1.25e-12

FYVE domain found in RUN and FYVE domain-containing protein 1 (RUFY1) and similar proteins; RUFY1, also termed 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 homologue 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.


Pssm-ID: 277297 [Multi-domain]  Cd Length: 71  Bit Score: 64.32  E-value: 1.25e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 157738667 1170 WLGDTEANHCLDCKREFSWMVRRHHCRICGRIFCYYCCNNYVLSKHGGKKERCCRAC 1226
Cdd:cd15758     6 WLKDDEATHCKQCEKEFSISRRKHHCRNCGHIFCNTCSSNELALPSYPKPVRVCDSC 62
FYVE_Hrs cd15720
FYVE domain found in hepatocyte growth factor (HGF)-regulated tyrosine kinase substrate (Hrs) ...
 1174-1230 1.40e-12

FYVE domain found in hepatocyte growth factor (HGF)-regulated tyrosine kinase substrate (Hrs) and similar proteins; Hrs, also termed protein pp110, is a tyrosine phosphorylated protein that plays an important role in the signaling pathway of HGF. It is localized to early endosomes and an essential component of the endosomal sorting and trafficking machinery. Hrs interacts with hypertonia-associated protein Trak1, a novel regulator of endosome-to-lysosome trafficking. It can also forms an Hrs/actinin-4/BERP/myosin V protein complex that is required for efficient transferrin receptor (TfR) recycling but not for epidermal growth factor receptor (EGFR) degradation. Moreover, Hrs, together with STAM proteins, STAM1 and STAM2, and EPs15, forms a multivalent ubiquitin-binding complex that sorts ubiquitinated proteins into the multivesicular body pathway, and plays a regulatory role in endocytosis/exocytosis. Furthermore, Hrs functions as an interactor of the neurofibromatosis 2 tumor suppressor protein schwannomin/merlin. It is also involved in the inhibition of citron kinase-mediated HIV-1 budding. Hrs contains a single ubiquitin-interacting motif (UIM) that is crucial for its function in receptor sorting, and a FYVE domain that harbors double Zn2+ binding sites.


Pssm-ID: 277260 [Multi-domain]  Cd Length: 61  Bit Score: 63.94  E-value: 1.40e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 157738667 1174 TEANHCLDCKREFSWMVRRHHCRICGRIFCYYCCNNY-VLSKHGGKKE-RCCRACFQKL 1230
Cdd:cd15720     3 KDGDECHRCRVQFGVFQRKHHCRACGQVFCGKCSSKSsTIPKFGIEKEvRVCDPCYEKL 61
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 611-995 2.18e-12

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: 72.41  E-value: 2.18e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   611 EEELRQANRELEKELQNVvGRNQLLEG----KLQALQAD------YQALQQRESAIQGSLASLEaeqasirhlgdqmeas 680
Cdd:TIGR02169  169 DRKKEKALEELEEVEENI-ERLDLIIDekrqQLERLRRErekaerYQALLKEKREYEGYELLKE---------------- 231

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   681 LLAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEVEQCQQLAEARHRELRALESQCQQQTQlievltaekgqqgvgppt 760
Cdd:TIGR02169  232 KEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVK------------------ 293

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   761 dNEARELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAkmraaldDQDKVQSQLSMAEAVLREHKTLVQQLKEqnEALNRA 840
Cdd:TIGR02169  294 -EKIGELEAEIASLERSIAEKERELEDAEERLAKLEA-------EIDKLLAEIEELEREIEEERKRRDKLTE--EYAELK 363

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   841 HVQELLQCSeregaLQEERADEAQQREEeLRALQEELSQAKCSSEEAQLEHAELQEQLHRANTDTAELGIQvcaLTVEKE 920
Cdd:TIGR02169  364 EELEDLRAE-----LEEVDKEFAETRDE-LKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAA---IAGIEA 434

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157738667   921 RVEEaLACAVQELQDAKEAASREREGLERQVAGLQQEKESLQEKLKAAKAAagsLPGLQAQLAQAEQRAQSLQEA 995
Cdd:TIGR02169  435 KINE-LEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKE---LSKLQRELAEAEAQARASEER 505
mukB PRK04863
chromosome partition protein MukB;
584-962 2.33e-12

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 72.30  E-value: 2.33e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  584 AWGKPEEEQRGLQEAQLddtkvqegSQEEELRQANRELEKE---LQNVVGRNQLLEGKLQALQADYQALQQRESAIQGSL 660
Cdd:PRK04863  273 DYMRHANERRVHLEEAL--------ELRRELYTSRRQLAAEqyrLVEMARELAELNEAESDLEQDYQAASDHLNLVQTAL 344

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  661 ASLEAE---QASIRHLGDQMEASLLAVRKAKEamkaQMAEKEAILQSKEGECQQLREEVEQCQQLAEARHRE-------L 730
Cdd:PRK04863  345 RQQEKIeryQADLEELEERLEEQNEVVEEADE----QQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRaiqyqqaV 420

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  731 RALESqCQQQTQL-----------IEVLTAEKGQQgvgpptDNEARELAAQLALSQAQLEVHQ----------GEVQRLQ 789
Cdd:PRK04863  421 QALER-AKQLCGLpdltadnaedwLEEFQAKEQEA------TEELLSLEQKLSVAQAAHSQFEqayqlvrkiaGEVSRSE 493

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  790 AQVVdlqakMRAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNEAlnrahvQELLQCSEREGALQEERADEAQQREEE 869
Cdd:PRK04863  494 AWDV-----ARELLRRLREQRHLAEQLQQLRMRLSELEQRLRQQQRA------ERLLAEFCKRLGKNLDDEDELEQLQEE 562

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  870 LRALQEELSQAKCSSEEAQLEHAELQEQL--------------HRANTDTAELGIQVCALTVEKERVEEALacavQELQD 935
Cdd:PRK04863  563 LEARLESLSESVSEARERRMALRQQLEQLqariqrlaarapawLAAQDALARLREQSGEEFEDSQDVTEYM----QQLLE 638

                         410       420
                  ....*....|....*....|....*..
gi 157738667  936 AKEAASREREGLERQVAGLQQEKESLQ 962
Cdd:PRK04863  639 RERELTVERDELAARKQALDEEIERLS 665
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
331-880 2.78e-12

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 71.87  E-value: 2.78e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  331 EDYHTALRRLE---SMLQPL---AQELEATRDSLDKKNQHLASFPGWlaMAQQKADTASDTKGRQEPIPSDAAQEMQELG 404
Cdd:COG4913   238 ERAHEALEDAReqiELLEPIrelAERYAAARERLAELEYLRAALRLW--FAQRRLELLEAELEELRAELARLEAELERLE 315

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  405 EKLQALERERTKVEEVNRQQS--------AQLEQLVKELQLKEDARASLERLVKEmapLQEELSGkgqEADQLWRRLQEL 476
Cdd:COG4913   316 ARLDALREELDELEAQIRGNGgdrleqleREIERLERELEERERRRARLEALLAA---LGLPLPA---SAEEFAALRAEA 389

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  477 LAHTSSWEEELAELRREkkqqqeekelleqeVRSLTRQLQFLETQLAQVSQHVSDLEEQKK----QLIQDKDHLSQQVGM 552
Cdd:COG4913   390 AALLEALEEELEALEEA--------------LAEAEAALRDLRRELRELEAEIASLERRKSnipaRLLALRDALAEALGL 455

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  553 LERlagppgpELPVAGEkneaLVPVnsslqeawgKPEEEQ-RGLQEAQLddtkvqeGSQ-------EEELRQANReleke 624
Cdd:COG4913   456 DEA-------ELPFVGE----LIEV---------RPEEERwRGAIERVL-------GGFaltllvpPEHYAAALR----- 503

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  625 lqnVVGRNQLlEGKLQALQAD-YQALQQRESAIQGSLAS-LEAEQASIR-----HLGDQM-------EASLLAVRKA--K 688
Cdd:COG4913   504 ---WVNRLHL-RGRLVYERVRtGLPDPERPRLDPDSLAGkLDFKPHPFRawleaELGRRFdyvcvdsPEELRRHPRAitR 579

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  689 EAM---KAQMAEK----------------EAILQSKEGECQQLREEVEQCQQLAEARHRELRALESQCQQQTQLIEVLTA 749
Cdd:COG4913   580 AGQvkgNGTRHEKddrrrirsryvlgfdnRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWD 659

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  750 EKGQQGVgpptDNEARELAAQLAlsqaQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAVLREHKTLVQQ 829
Cdd:COG4913   660 EIDVASA----EREIAELEAELE----RLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDE 731

                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|....
gi 157738667  830 LKEQNEALNRAHVQELLQCSE--REGALQEERADEAQQR-EEELRALQEELSQA 880
Cdd:COG4913   732 LQDRLEAAEDLARLELRALLEerFAAALGDAVERELRENlEERIDALRARLNRA 785
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 857-1169 3.59e-12

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 71.51  E-value: 3.59e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  857 EERADEAQQREEELRALQEELsqakcsseEAQLEHAELQ-EQLHRANTDTAELGI-QVCALTVEKERVEEALACAVQELQ 934
Cdd:COG1196   178 ERKLEATEENLERLEDILGEL--------ERQLEPLERQaEKAERYRELKEELKElEAELLLLKLRELEAELEELEAELE 249

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  935 DAKEAASREREGLERQVAGLQQEKESLQEKLKAAKAAAGSLPGLQAQLAQAEQRAQSLQEAAHQELNTLKfQLSAEIMDY 1014
Cdd:COG1196   250 ELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLE-ELEEELAEL 328

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667 1015 QSRLKNAGEECKSLRGQLEEQGRQLQAAEEAVEKLKATQADMGEKLSCTSNHLAECQAAMLRKDKEGAALREDLERTQKE 1094
Cdd:COG1196   329 EEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEA 408

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157738667 1095 LEKATTKIQEYYnklcQEVTNRERNDQKMLADLDDLNRTKKYLEERLIELLRDKDALWQKSDALEFQQKLSAEER 1169
Cdd:COG1196   409 EEALLERLERLE----EELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAAL 479
FYVE_RUFY4 cd15745
FYVE-related domain found in RUN and FYVE domain-containing protein 4 (RUFY4) and similar ...
 1178-1227 5.85e-12

FYVE-related domain found in RUN and FYVE domain-containing protein 4 (RUFY4) and similar proteins; 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. The FYVE domain of RUFY4 resembles the FYVE-related domain as it lacks the WxxD motif (x for any residue). The biological function of RUFY4 still remains unclear.


Pssm-ID: 277284 [Multi-domain]  Cd Length: 52  Bit Score: 61.75  E-value: 5.85e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 157738667 1178 HCLDCKREFSWMVRRHHCRICGRIFCYYCCNNYVLSKH--GGKKERCCRACF 1227
Cdd:cd15745     1 ACAICAKAFSLFRRKYVCRLCGGVVCHSCSSEDLVLSVpdTCIYLRVCKTCY 52
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 315-1007 5.90e-12

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 70.77  E-value: 5.90e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   315 LQTCLQGLELGAAEKEEDYHTALRRLESMLQPLAQELEATRDSLDKKNQHLASFPGWLAMAQQKADTASDTKGRQEPIPS 394
Cdd:TIGR00618  199 LTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAV 278

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   395 DA-AQEMQELGEKLQALERERTKVEEVNRQQSAQLEQLVKELQLKEDARASLERLVKEMAPLQEElsgkgQEADQLWRRL 473
Cdd:TIGR00618  279 LEeTQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQ-----RRLLQTLHSQ 353

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   474 QELLAhtssweeelaelrrekkqqqeekelleqevRSLTRQLQFLETQLAQVS--QHVSDLEEQKKQLIQDKDHLSQQVG 551
Cdd:TIGR00618  354 EIHIR------------------------------DAHEVATSIREISCQQHTltQHIHTLQQQKTTLTQKLQSLCKELD 403

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   552 MLERLAGPPGPELpvageknEALVPVNSSLQEAWGKPEEEQRGLQEAQLDDTKV-QEGSQEE----ELRQANRELEKELQ 626
Cdd:TIGR00618  404 ILQREQATIDTRT-------SAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTaQCEKLEKihlqESAQSLKEREQQLQ 476

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   627 NVVGRNQLLEGKLQALQADYQALQQRESAIQGSLASLEAEQASIRHLGdqmeasllAVRKAKEAMKAQMAEKEAILQSKE 706
Cdd:TIGR00618  477 TKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPG--------PLTRRMQRGEQTYAQLETSEEDVY 548

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   707 GECQQLREEVEQCQQLAEARHRELRALESQCQQQTQLIEVLTAEkgQQGVGPPTDNEARELAAQLALSQAQLEVHQGEVQ 786
Cdd:TIGR00618  549 HQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNI--TVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQD 626

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   787 RLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNEALNRAHVQELLQCSEREGALQEERAD----- 861
Cdd:TIGR00618  627 LQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQcqtll 706

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   862 -EAQQREEELRALQEELSQAKcSSEEAQLEhAELQEQLHRANTDTAELGIQVCALTVEKERVEEALACAVQ---ELQDAK 937
Cdd:TIGR00618  707 rELETHIEEYDREFNEIENAS-SSLGSDLA-AREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQtgaELSHLA 784

                          650       660       670       680       690       700       710
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   938 EAASREREGLERQVAGLQQEKESLQEKLkaaKAAAGSLPGLQAQLAQAEQRAQSLQEAAHQELNTLKFQL 1007
Cdd:TIGR00618  785 AEIQFFNRLREEDTHLLKTLEAEIGQEI---PSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQL 851
RUN_RUNDC3 cd17684
RUN domain found in RUN domain-containing protein 3 (RUNDC3) and similar proteins; RUNDC3 ...
 33-135 5.99e-12

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: 65.11  E-value: 5.99e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   33 EPITDDSTSLHKFSYKLEYLLQFDQKEKATLLGN--KKDYWDYFCACLAKVkgANDGIRFVKSISELRTSLGKGRAFIRY 110
Cdd:cd17684    20 ETIDDSSEELINFAAILEQILSHRLKPVKPWYGSeePRTFWDYIRVACKKV--PQNCIASIEQMENIKSPKAKGRAWIRV 97

                          90       100
                  ....*....|....*....|....*
gi 157738667  111 SLVHQRLADTLQQCFMNTKVTSDWY 135
Cdd:cd17684    98 ALMEKRLSEYLSTALKQTRLTRNFY 122
FYVE_RABE_unchar cd15739
FYVE domain found in uncharacterized rab GTPase-binding effector proteins from bilateria; This ...
 1167-1227 6.83e-12

FYVE domain found in uncharacterized rab GTPase-binding effector proteins from bilateria; This family includes a group of uncharacterized rab GTPase-binding effector proteins found in bilateria. Although their biological functions remain unclear, they all contain a FYVE domain that harbors a putative phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) binding site.


Pssm-ID: 277278 [Multi-domain]  Cd Length: 73  Bit Score: 62.36  E-value: 6.83e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157738667 1167 EERWLGDTEANHCLDCKREFSWMVRRHHCRICGRIFCYYCCNNYVLSKHGGKKERCCRACF 1227
Cdd:cd15739     1 EVRWQHEDDVDQCPNCKTPFSVGKRKHHCRHCGKIFCSDCLTKTVPSGPNRRPARVCDVCH 61
FYVE_PKHF cd15717
FYVE domain found in protein containing both PH and FYVE domains 1 (phafin-1), 2 (phafin-2), ...
 1170-1227 1.02e-11

FYVE domain found in protein containing both PH and FYVE domains 1 (phafin-1), 2 (phafin-2), and similar proteins; This family includes protein containing both PH and FYVE domains 1 (phafin-1) and 2 (phafin-2). Phafin-1 is a representative of a novel family of PH and FYVE domain-containing proteins called phafins. It is a ubiquitously expressed pro-apoptotic protein via translocating to lysosomes, facilitating apoptosis induction through a lysosomal-mitochondrial apoptotic pathway. Phafin-2 is a ubiquitously expressed endoplasmic reticulum-associated protein that facilitates tumor necrosis factor alpha (TNF-alpha)-triggered cellular apoptosis through endoplasmic reticulum (ER)-mitochondrial apoptotic pathway. It is an endosomal phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) effector, as well as an interactor of the endosomal-tethering protein EEA1. It regulates endosome fusion upstream of Rab5. Phafin-2 also functions as a novel regulator of endocytic epidermal growth factor receptor (EGFR) degradation through a role in endosomal fusion.


Pssm-ID: 277257 [Multi-domain]  Cd Length: 61  Bit Score: 61.23  E-value: 1.02e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667 1170 WLGDTEANHCLDCKR-EFSWMVRRHHCRICGRIFCYYCCNNYVLSKHGGKKE-RCCRACF 1227
Cdd:cd15717     2 WVPDSEAPVCMHCKKtKFTAINRRHHCRKCGAVVCGACSSKKFLLPHQSSKPlRVCDTCY 61
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 234-1034 1.12e-11

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: 69.98  E-value: 1.12e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  234 EMRLELDQLEVREKQLRERMQQLDRENQELRAAVSQQgEQLQTERERGRTAAEDNVRLTCLVAELQKQWEVTQA----TQ 309
Cdd:COG3096   310 EMARELEELSARESDLEQDYQAASDHLNLVQTALRQQ-EKIERYQEDLEELTERLEEQEEVVEEAAEQLAEAEArleaAE 388

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  310 NTVKELQTCL----QGLELgAAEKEEDYHTALRRLESmlqplAQELeatrdsLDKKNQHLASFPGWLAMAQQKADTASDT 385
Cdd:COG3096   389 EEVDSLKSQLadyqQALDV-QQTRAIQYQQAVQALEK-----ARAL------CGLPDLTPENAEDYLAAFRAKEQQATEE 456

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  386 KGRQEPIPSDAAQEMQELGEKLQALERertKVEEVNRQQSAQLEQlvkelQLKEDARaSLERLVKEMAPLQEELSgkgqE 465
Cdd:COG3096   457 VLELEQKLSVADAARRQFEKAYELVCK---IAGEVERSQAWQTAR-----ELLRRYR-SQQALAQRLQQLRAQLA----E 523

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  466 ADQLWRRLQELlahtssweeelaelRREKKQQQEEKELLEQEVRSLTRQLQFLETQLAQVSQHVSDLEEQKKQLIQDKDH 545
Cdd:COG3096   524 LEQRLRQQQNA--------------ERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQ 589

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  546 LSQQVGMLERLAgppgpelPVAGEKNEALvpvnSSLQEAWGKPEEEQRGLQEA--QLDDTKVQEGSQEEELRQANRELEK 623
Cdd:COG3096   590 LRARIKELAARA-------PAWLAAQDAL----ERLREQSGEALADSQEVTAAmqQLLEREREATVERDELAARKQALES 658

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  624 ELQNVVGRNQLLEGKLQALQADYQALQQRE-------------SAIQGSLAS------LEAEQASIRHLGDQMEASLL-- 682
Cdd:COG3096   659 QIERLSQPGGAEDPRLLALAERLGGVLLSEiyddvtledapyfSALYGPARHaivvpdLSAVKEQLAGLEDCPEDLYLie 738

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  683 --------AVRKAKEAMKAQMA--EKEAILQSKEGEC------------QQLREEVEQcqqLAEaRHRELRALESQCQQQ 740
Cdd:COG3096   739 gdpdsfddSVFDAEELEDAVVVklSDRQWRYSRFPEVplfgraarekrlEELRAERDE---LAE-QYAKASFDVQKLQRL 814

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  741 TQLIEVLTAEKGQQGVGPPTDNEARELAAQLALSQAQLEVHQGEVQRLQAQVVDLqakmRAALDDQDKVQSQLS-MAEAV 819
Cdd:COG3096   815 HQAFSQFVGGHLAVAFAPDPEAELAALRQRRSELERELAQHRAQEQQLRQQLDQL----KEQLQLLNKLLPQANlLADET 890

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  820 LREhktLVQQLKEQNEALNRAhVQELLQCSEREGALqEERADEAQQREEELRALQEELSQAKCSSEEAQLEHAEL----Q 895
Cdd:COG3096   891 LAD---RLEELREELDAAQEA-QAFIQQHGKALAQL-EPLVAVLQSDPEQFEQLQADYLQAKEQQRRLKQQIFALsevvQ 965

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  896 EQLHRANTDTAELGIQVCALTvekERVEEALACAVQELQDAKEAASREREGLERQVAGLQQEKESLQEKLKAAKAAAGSL 975
Cdd:COG3096   966 RRPHFSYEDAVGLLGENSDLN---EKLRARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQEL 1042

                         810       820       830       840       850       860       870
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  976 PGLQAQL-AQAEQRAQSLQEAAHQELNTLKFQLS----------AEIMDYQSRLKNAGEECKSLRGQLEE 1034
Cdd:COG3096  1043 EELGVQAdAEAEERARIRRDELHEELSQNRSRRSqlekqltrceAEMDSLQKRLRKAERDYKQEREQVVQ 1112
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 238-1104 1.37e-11

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: 69.43  E-value: 1.37e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   238 ELDQLEVREKQLRERMQQLDRENQELRAAVSQQGEQLQTERERGRTAAEDNVRLTC-----------LVAELQKQWEVTQ 306
Cdd:pfam01576   13 ELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAArkqeleeilheLESRLEEEEERSQ 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   307 ATQNTVKELQTCLQGLElGAAEKEEDYHTALR----RLESMLQPLAQELEATRDSLDKKN-------QHLASFPGWLAMA 375
Cdd:pfam01576   93 QLQNEKKKMQQHIQDLE-EQLDEEEAARQKLQlekvTTEAKIKKLEEDILLLEDQNSKLSkerklleERISEFTSNLAEE 171

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   376 QQKADTASDTKGRQEPIPSDAAQEMQELGEKLQALERERTKVEevnrQQSAQLEQLVKELQLK-EDARASLERLVKEMAP 454
Cdd:pfam01576  172 EEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLE----GESTDLQEQIAELQAQiAELRAQLAKKEEELQA 247

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   455 LQEELSGKGQEADQLWRRLQELLAHTSSWEEELAELRREKKQQQEEKELLEQEVRSLTRQLQ-FLETQLAQV---SQHVS 530
Cdd:pfam01576  248 ALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEdTLDTTAAQQelrSKREQ 327

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   531 DLEEQKKQLIQDKDHLSQQVGMLERlagppgpelpvagEKNEALVPVNSSLqeawgkpeeEQRGLQEAQLDDTKVQEGSQ 610
Cdd:pfam01576  328 EVTELKKALEEETRSHEAQLQEMRQ-------------KHTQALEELTEQL---------EQAKRNKANLEKAKQALESE 385

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   611 EEELRQANRELEKELQNVVGRNQLLEGKLQALQADYQALQQRESAIQGSLASLEAEQASIRHLGDQMEASLLAVRKAKEA 690
Cdd:pfam01576  386 NAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSS 465

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   691 MKAQMAEKEAILQ-------SKEGECQQLREEVEQCQQLAEARHRELRALESQCQQ-QTQLIEVLTAEKGQQGVGPPTDN 762
Cdd:pfam01576  466 LESQLQDTQELLQeetrqklNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTlQAQLSDMKKKLEEDAGTLEALEE 545

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   763 EARELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEavlREHKTLVQQLKEQNEALNRAhv 842
Cdd:pfam01576  546 GKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLE---KKQKKFDQMLAEEKAISARY-- 620

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   843 qellqCSEREGAlqeeradEAQQREEELRALQeeLSQAkcsSEEAQlehaELQEQLHRANTdtaELGIQVCALTVEKERV 922
Cdd:pfam01576  621 -----AEERDRA-------EAEAREKETRALS--LARA---LEEAL----EAKEELERTNK---QLRAEMEDLVSSKDDV 676

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   923 EEalacAVQELQDAKEAasreregLERQVAGLQQEKESLQEKLKAAKAAAGSLP-GLQAQLAQAEQRAQSLQEAAHQELN 1001
Cdd:pfam01576  677 GK----NVHELERSKRA-------LEQQVEEMKTQLEELEDELQATEDAKLRLEvNMQALKAQFERDLQARDEQGEEKRR 745

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  1002 TLKFQ---LSAEIMDYQSRLKNAGEECKSLRGQLEEQGRQLQAA----EEAVEKLKATQADMGEklsctsnHLAECQAAM 1074
Cdd:pfam01576  746 QLVKQvreLEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAAnkgrEEAVKQLKKLQAQMKD-------LQRELEEAR 818

                          890       900       910
                   ....*....|....*....|....*....|
gi 157738667  1075 LRKDKEGAALREDlERTQKELEKATTKIQE 1104
Cdd:pfam01576  819 ASRDEILAQSKES-EKKLKNLEAELLQLQE 847
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 867-1176 3.13e-11

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: 68.56  E-value: 3.13e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   867 EEELRALQEELSQAKCSSEEAQLEHAELQEQLHRANTDTAELgIQVCALTVEKERVEealacaVQELQDAKEAASREREG 946
Cdd:TIGR02169  169 DRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKA-ERYQALLKEKREYE------GYELLKEKEALERQKEA 241

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   947 LERQVAGLQQEKESLQEKLKAAKAAAGSLPGLQAQLAQ-----AEQRAQSLQEAAHqELNTLKFQLSAEIMDYQSRLKNA 1021
Cdd:TIGR02169  242 IERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKkikdlGEEEQLRVKEKIG-ELEAEIASLERSIAEKERELEDA 320

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  1022 GEECKSLRGQLEEQGRQLQAAEEAVEKLKATQADMGEKLSCTSNHLAECQAAMLRKDKEGAALREDLERTQKELEKATTK 1101
Cdd:TIGR02169  321 EERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKRE 400

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  1102 IqeyyNKLCQEVTNRERNDQKMLADLDDLNRTKKYLEERLIELLRDKDALWQKSDALE-----FQQKLSAEERWLGDTEA 1176
Cdd:TIGR02169  401 I----NELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEwkleqLAADLSKYEQELYDLKE 476
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 226-887 3.17e-11

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: 68.54  E-value: 3.17e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   226 NEALEGFDEMRLELDQLEVREKQLRERMQQLDRENQELRAAVSQQGEQLQTERERGRTAAEdnvRLTCLVAELQKQWEVT 305
Cdd:TIGR02168  347 EELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEA---RLERLEDRRERLQQEI 423

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   306 QATQNTVKELQtcLQGLELGAAEKEEDYHTALRRLESmlqpLAQELEATRDSLDKKNQHLASFPGWLAMAQQKADTASDT 385
Cdd:TIGR02168  424 EELLKKLEEAE--LKELQAELEELEEELEELQEELER----LEEALEELREELEEAEQALDAAERELAQLQARLDSLERL 497

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   386 KGRQEPIPSDAAQEMQE----------------------------LGEKLQAL------------------ERERTKVEE 419
Cdd:TIGR02168  498 QENLEGFSEGVKALLKNqsglsgilgvlselisvdegyeaaieaaLGGRLQAVvvenlnaakkaiaflkqnELGRVTFLP 577

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   420 VNRQQSAQLEQLVKE-LQLKEDARASLERLVKEMAPLQEELSG---------KGQEADQLWRRLQ----------ELLAH 479
Cdd:TIGR02168  578 LDSIKGTEIQGNDREiLKNIEGFLGVAKDLVKFDPKLRKALSYllggvlvvdDLDNALELAKKLRpgyrivtldgDLVRP 657

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   480 TSSWEEELAELRREKKQQQEEKELLEQEVRSLTRQLQFLETQLAQVSQHVSDLEEQKKQLIQDKDHLSQQVGMLERlagp 559
Cdd:TIGR02168  658 GGVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRK---- 733

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   560 pgpELPVAGEKNEALVPVNSSLQEAWGKPEEeqrglQEAQLDDTKVQEGSQEEELRQANRELEKELQNVVGRNQLLEGKL 639
Cdd:TIGR02168  734 ---DLARLEAEVEQLEERIAQLSKELTELEA-----EIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREAL 805

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   640 QALQADYQALQQRESAIQGSLASLEAEQASIrhlgdqmEASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEVEQC 719
Cdd:TIGR02168  806 DELRAELTLLNEEAANLRERLESLERRIAAT-------ERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEAL 878

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   720 QQLAEARHRELRALESQCQQQTQLIEVLTAEKGQqgvgppTDNEARELAAQLALSQAQLEVHQGEVQRLQAQV-VDLQAK 798
Cdd:TIGR02168  879 LNERASLEEALALLRSELEELSEELRELESKRSE------LRRELEELREKLAQLELRLEGLEVRIDNLQERLsEEYSLT 952

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   799 MRAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNEAlnrahvqellqcseregALQEerADEAQQREEELRALQEELS 878
Cdd:TIGR02168  953 LEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLA-----------------AIEE--YEELKERYDFLTAQKEDLT 1013


                   ....*....
gi 157738667   879 QAKCSSEEA 887
Cdd:TIGR02168 1014 EAKETLEEA 1022
FYVE_RBNS5 cd15716
FYVE domain found in FYVE finger-containing Rab5 effector protein rabenosyn-5 (Rbsn-5) and ...
 1170-1231 3.58e-11

FYVE domain found in FYVE finger-containing Rab5 effector protein rabenosyn-5 (Rbsn-5) and similar proteins; Rbsn-5, also termed zinc finger FYVE domain-containing protein 20, is a novel Rab5 effector that is complexed to the Sec1-like protein VPS45 and recruited in a phosphatidylinositol-3-kinase-dependent fashion to early endosomes. It also binds to Rab4 and EHD1/RME-1, two regulators of the recycling route, and is involved in cargo recycling to the plasma membrane. Moreover, Rbsn-5 regulates endocytosis at the apical side of the wing epithelium and plays a role of the apical endocytic trafficking of Fmi in the establishment of planar cell polarity (PCP).


Pssm-ID: 277256 [Multi-domain]  Cd Length: 61  Bit Score: 59.66  E-value: 3.58e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157738667 1170 WLGDTEANHCLDCKREFSWMVRRHHCRICGRIFCYYCcnnyvlSKHGGKKERCCRACFQKLS 1231
Cdd:cd15716     4 WVNDSDVPFCPDCGKKFNLARRRHHCRLCGSIMCNKC------SQFLPLHIRCCHHCKDLLE 59
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
581-996 3.78e-11

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 67.87  E-value: 3.78e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  581 LQEAWGKPEEEQRGLQEAQLDDTKVQEGSQE-EELRQANRELEKELQN--VVGRNQLLEGKLQALQADYQALQQRESAIQ 657
Cdd:COG4717    80 LKEAEEKEEEYAELQEELEELEEELEELEAElEELREELEKLEKLLQLlpLYQELEALEAELAELPERLEELEERLEELR 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  658 GSLASLEAEQASIRHLGDQMEAsllAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEVEQCQQLAEARHRELRALESQC 737
Cdd:COG4717   160 ELEEELEELEAELAELQEELEE---LLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENEL 236

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  738 ---------QQQTQLIEVLTAEKGQQGVGPPTDNEARELAAQLALS-------------QAQLEVHQGEVQRLQAQVVDL 795
Cdd:COG4717   237 eaaaleerlKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVlgllallflllarEKASLGKEAEELQALPALEEL 316

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  796 QAKMRAALDDQDKVQSQLS--MAEAVLREHKTLVQQLKEQNEALNRAHVQELLQcsEREGALQEERADEaqqrEEELRAL 873
Cdd:COG4717   317 EEEELEELLAALGLPPDLSpeELLELLDRIEELQELLREAEELEEELQLEELEQ--EIAALLAEAGVED----EEELRAA 390

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  874 QEELSQAkcssEEAQLEHAELQEQLHRANTDTAELgiqvcALTVEKERVEEALacavQELQDAKEAASREREGLERQVAG 953
Cdd:COG4717   391 LEQAEEY----QELKEELEELEEQLEELLGELEEL-----LEALDEEELEEEL----EELEEELEELEEELEELREELAE 457

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|...
gi 157738667  954 LQQEKESLQEKlkaakaaaGSLPGLQAQLAQAEQRAQSLQEAA 996
Cdd:COG4717   458 LEAELEQLEED--------GELAELLQELEELKAELRELAEEW 492
FYVE_ZFYV1 cd15734
FYVE domains found in zinc finger FYVE domain-containing protein 1 (ZFYV1) and similar ...
 1170-1227 4.34e-11

FYVE domains found in zinc finger FYVE domain-containing protein 1 (ZFYV1) and similar proteins; ZFYV1, also termed double FYVE-containing protein 1 (DFCP1), or SR3, or tandem FYVE fingers-1, is a novel tandem FYVE domain containing protein that binds phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) with high specificity over other phosphoinositides. The subcellular distribution of exogenously-expressed ZFYV1 to Golgi, endoplasmic reticulum (ER) and vesicular is governed in part by its FYVE domains but unaffected by wortmannin, a PI3-kinase inhibitor. In addition to C-terminal tandem FYVE domain, ZFYV1 contains an N-terminal putative C2H2 type zinc finger and a possible nucleotide binding P-loop.


Pssm-ID: 277273 [Multi-domain]  Cd Length: 61  Bit Score: 59.65  E-value: 4.34e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667 1170 WLGDTEANHCLDCKREFSWMVRRHHCRICGRIFCYYCCNNYVLSKHGGKKE--RCCRACF 1227
Cdd:cd15734     2 WVPDSEIKECSVCKRPFSPRLSKHHCRACGQGVCDDCSKNRRPVPSRGWDHpvRVCDPCA 61
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
784-1046 7.80e-11

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 67.25  E-value: 7.80e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  784 EVQRLQAQVVDLQAKMRAALDDQDKVQsQLSMAEAVLREHKTLVQQLKEQNEALNRAHVQEllqcSEREGALQEERADEA 863
Cdd:COG4913   226 AADALVEHFDDLERAHEALEDAREQIE-LLEPIRELAERYAAARERLAELEYLRAALRLWF----AQRRLELLEAELEEL 300

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  864 qqrEEELRALQEELSQAKCSSEEAQLEHAELQEQLHRANTDT-AELGIQVCALTVEKERVEEALACAVQELQDAKEAASR 942
Cdd:COG4913   301 ---RAELARLEAELERLEARLDALREELDELEAQIRGNGGDRlEQLEREIERLERELEERERRRARLEALLAALGLPLPA 377

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  943 EREGLERQVAGLQQEKESLQEKLKAakaaagslpgLQAQLAQAEQRAQSLQEAAHQelntlkfqLSAEIMDYQSRLKNAG 1022
Cdd:COG4913   378 SAEEFAALRAEAAALLEALEEELEA----------LEEALAEAEAALRDLRRELRE--------LEAEIASLERRKSNIP 439

                         250       260
                  ....*....|....*....|....
gi 157738667 1023 EECKSLRGQLEEqgrQLQAAEEAV 1046
Cdd:COG4913   440 ARLLALRDALAE---ALGLDEAEL 460
mukB PRK04863
chromosome partition protein MukB;
654-1097 9.40e-11

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 66.90  E-value: 9.40e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  654 SAIQGSLAS-LEAEQASIRHLGDQMEASLLAVRKAKEAMKaqmaekeaILQSKEGECQQLREEVEQCQQLAEARHRELRA 732
Cdd:PRK04863  211 SAITRSLRDyLLPENSGVRKAFQDMEAALRENRMTLEAIR--------VTQSDRDLFKHLITESTNYVAADYMRHANERR 282

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  733 LESQcqqqtqliEVLTAEKGQQGvgpptdneARElaaQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQ 812
Cdd:PRK04863  283 VHLE--------EALELRRELYT--------SRR---QLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQTA 343

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  813 LSMAEAVLR---EHKTLVQQLKEQNEAlnRAHVQELLQCSEREGALQEERADEA-------QQREEEL--RALQEElsQA 880
Cdd:PRK04863  344 LRQQEKIERyqaDLEELEERLEEQNEV--VEEADEQQEENEARAEAAEEEVDELksqladyQQALDVQqtRAIQYQ--QA 419

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  881 KCSSEEAQlehaelqEQLHRANTDTAELGIQVCALTVEKERVEEALACAVQELQDAKEAASREREGLE--RQVAG----- 953
Cdd:PRK04863  420 VQALERAK-------QLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQlvRKIAGevsrs 492

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  954 -LQQEKESLQEKLKAAKAAAGSLPGLQAQLAQAEQRAQSLQEA----------------AHQELNTLKFQLSAEIMDYQS 1016
Cdd:PRK04863  493 eAWDVARELLRRLREQRHLAEQLQQLRMRLSELEQRLRQQQRAerllaefckrlgknldDEDELEQLQEELEARLESLSE 572

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667 1017 RLKNAGEECKSLRGQLEEQGRQLQ----------AAEEAVEKLkatQADMGEKLScTSNHLAECQAAMLRKDKEGAALRE 1086
Cdd:PRK04863  573 SVSEARERRMALRQQLEQLQARIQrlaarapawlAAQDALARL---REQSGEEFE-DSQDVTEYMQQLLERERELTVERD 648

                         490
                  ....*....|.
gi 157738667 1087 DLERTQKELEK 1097
Cdd:PRK04863  649 ELAARKQALDE 659
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
509-1056 1.12e-10

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 66.60  E-value: 1.12e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  509 RSLTRQLQFLETQLAQVSQHVSDLEEQKKQLIQDKDHLSQqvgMLERLAgppgpelpvagEKNEALVPVnsslqeawgkp 588
Cdd:PRK02224  202 KDLHERLNGLESELAELDEEIERYEEQREQARETRDEADE---VLEEHE-----------ERREELETL----------- 256

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  589 EEEQRGLQEAQLDDTKVQEGSQEE--ELRQANRELEKELQNVVGRNQLLEGKLQALQADYQALQQRESAIQGSLA----- 661
Cdd:PRK02224  257 EAEIEDLRETIAETEREREELAEEvrDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEecrva 336

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  662 --SLEAEQASIRHLGDQMEASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEVEQCQQL----------AEARHRE 729
Cdd:PRK02224  337 aqAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERfgdapvdlgnAEDFLEE 416

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  730 LRALESQCQQQTQLIEVlTAEKGQQGVgpptdNEARELAAQLALSQAQLEV----HQGEVQRLQAQVVDLQAKMRAALDD 805
Cdd:PRK02224  417 LREERDELREREAELEA-TLRTARERV-----EEAEALLEAGKCPECGQPVegspHVETIEEDRERVEELEAELEDLEEE 490

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  806 QDKVQSQLSMAEAvLREHKTLVQQLKEQNEAlnrahVQELLqcseregALQEERADEAQQREEELRALQEEL-SQAKCSS 884
Cdd:PRK02224  491 VEEVEERLERAED-LVEAEDRIERLEERRED-----LEELI-------AERRETIEEKRERAEELRERAAELeAEAEEKR 557

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  885 EEAQLEHAELQEQLHRAntdtAELGIQVCALTVEKERVEeALACAVQELQDAKEAASREREGLERQVAGLQQEKESLQEK 964
Cdd:PRK02224  558 EAAAEAEEEAEEAREEV----AELNSKLAELKERIESLE-RIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEK 632

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  965 LKAAKAAAGSLPGLQAQLAQAE-QRAQSLQEAAHQELNTL---KFQLSAEIMDYQSRLKNAgEECKSLRGQLEEQGRQLQ 1040
Cdd:PRK02224  633 RERKRELEAEFDEARIEEAREDkERAEEYLEQVEEKLDELreeRDDLQAEIGAVENELEEL-EELRERREALENRVEALE 711

                         570
                  ....*....|....*.
gi 157738667 1041 AAEEAVEKLKATQADM 1056
Cdd:PRK02224  712 ALYDEAEELESMYGDL 727
FYVE_RUFY2 cd15759
FYVE domain found in RUN and FYVE domain-containing protein 2 (RUFY2) and similar proteins; ...
 1170-1226 1.19e-10

FYVE domain found in RUN and FYVE domain-containing protein 2 (RUFY2) and similar proteins; RUFY2, also termed 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.


Pssm-ID: 277298 [Multi-domain]  Cd Length: 71  Bit Score: 58.88  E-value: 1.19e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 157738667 1170 WLGDTEANHCLDCKREFSWMVRRHHCRICGRIFCYYCCNNYVLSKHGGKKERCCRAC 1226
Cdd:cd15759     4 WLKDKEATHCKLCEKEFSLSKRKHHCRNCGEIFCNACSDNELPLPSSPKPVRVCDSC 60
FYVE2_Vac1p_like cd15737
FYVE domain 2 found in yeast protein VAC1 (Vac1p) and similar proteins; Vac1p, also termed ...
 1169-1203 1.81e-10

FYVE domain 2 found in yeast protein VAC1 (Vac1p) and similar proteins; Vac1p, also termed vacuolar segregation protein Pep7p, or carboxypeptidase Y-deficient protein 7, or vacuolar protein sorting-associated protein 19 (Vps19p), or vacuolar protein-targeting protein 19, is a phosphatidylinositol 3-phosphate (PtdIns3P or PI3P)-binding protein that interacts with a Rab GTPase, GTP-bound form of Vps21p, and a Sec1p homologue, Vps45p, to facilitate Vps45p-dependent vesicle-mediated vacuolar protein sorting. It also acts as a novel regulator of vesicle docking and/or fusion at the endosome and functions in vesicle-mediated transport of Golgi precursor carboxypeptidase Y (CPY), protease A (PrA), protease B (PrB), but not alkaline phosphatase (ALP) from the trans-Golgi network-like compartment (TGN) to the endosome. Vac1p contains an N-terminal classical TFIIIA-like zinc finger, two putative zinc-binding FYVE fingers, and a C-terminal coiled coil region. The family corresponds to the second FYVE domain that is responsible for the ability of Pep7p to efficiently interact with Vac1p and Vps45p.


Pssm-ID: 277276 [Multi-domain]  Cd Length: 83  Bit Score: 58.67  E-value: 1.81e-10
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 157738667 1169 RWLGDTEANHCLDCKREFSWMVRRHHCRICGRIFC 1203
Cdd:cd15737     1 PWEDDSSVTHCPICLRSFGLLLRKHHCRLCGKVVC 35
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 563-1176 2.14e-10

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: 65.86  E-value: 2.14e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   563 ELPVAGEKNEALVPVNSSLQEAWGKPEEEQRGLQEAQLDDTKVQEGSQEEELRQANrELEKELQNVVGRNQLLEGKLQAL 642
Cdd:TIGR02169  178 ELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKE-ALERQKEAIERQLASLEEELEKL 256

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   643 QADYQALQQRESAIQGSLASLEAEqasIRHLGdqmEASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEVEQCQQL 722
Cdd:TIGR02169  257 TEEISELEKRLEEIEQLLEELNKK---IKDLG---EEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAE 330

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   723 AEARHRELRALESQCQQQTQLIEVLTAE-KGQQGVGPPTDNEARELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRA 801
Cdd:TIGR02169  331 IDKLLAEIEELEREIEEERKRRDKLTEEyAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDR 410

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   802 ALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNEALN---RAHVQELLQCSE-REGALQEERADEAQQR--EEELRALQE 875
Cdd:TIGR02169  411 LQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKAleiKKQEWKLEQLAAdLSKYEQELYDLKEEYDrvEKELSKLQR 490

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   876 ELSQAkcsseEAQLEHAELQEQLHRANTDTAELGIQ-VCALTVEKERVEEALACAVQ-----ELQ----DAKEAASRERE 945
Cdd:TIGR02169  491 ELAEA-----EAQARASEERVRGGRAVEEVLKASIQgVHGTVAQLGSVGERYATAIEvaagnRLNnvvvEDDAVAKEAIE 565

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   946 GLERQVAGLQ--------QEKESLQEKLKAAKAAA--------------------------------------------- 972
Cdd:TIGR02169  566 LLKRRKAGRAtflplnkmRDERRDLSILSEDGVIGfavdlvefdpkyepafkyvfgdtlvvedieaarrlmgkyrmvtle 645

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   973 ------------GSLPGLQAQLAQAEQRAQSLQEAAH-QELNTLKFQLSAEIMDYQSRLKNAGEECKSLRGQLEEQGRQL 1039
Cdd:TIGR02169  646 gelfeksgamtgGSRAPRGGILFSRSEPAELQRLRERlEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEI 725

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  1040 QAAEEAVEKLKATQADMGEKLSCTSNHLAECQAAMLRKDKEGAALREDLERTQKELEKATT--------KIQEYYNKLCQ 1111
Cdd:TIGR02169  726 EQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEArlshsripEIQAELSKLEE 805

                          650       660       670       680       690       700
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157738667  1112 EVTNRERNDQKMLADLDDLNRTKKYLEERLIELLRDKDALwqKSDALEFQQKLSAEERWLGDTEA 1176
Cdd:TIGR02169  806 EVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDL--KEQIKSIEKEIENLNGKKEELEE 868
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
403-1050 2.27e-10

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 65.47  E-value: 2.27e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  403 LGEKLQALERERTKVEEVnRQQSAQLEQLVKElqlKEDARASLERLVKEMAPLQEELSGKGQEADQLWRRLQELlahtss 482
Cdd:PRK03918  167 LGEVIKEIKRRIERLEKF-IKRTENIEELIKE---KEKELEEVLREINEISSELPELREELEKLEKEVKELEEL------ 236

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  483 weeelaelRREKKQQQEEKELLEQEVRSLTRQLQFLETQLAQVSQHVSDLEEQKKQliqdkdhlsqqvgmLERLAGPPGP 562
Cdd:PRK03918  237 --------KEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKE--------------LKELKEKAEE 294

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  563 ELPVAGEKNEALVPVNsSLQEAWGKPEEEQRGLQEaqlddtKVQEGSQEEELRQANRELEKELQNVVGRnqlLEGKLQAL 642
Cdd:PRK03918  295 YIKLSEFYEEYLDELR-EIEKRLSRLEEEINGIEE------RIKELEEKEERLEELKKKLKELEKRLEE---LEERHELY 364

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  643 QaDYQALQQRESAIQGSLASLEAEQAsirhlgdqmEASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEVEqcqql 722
Cdd:PRK03918  365 E-EAKAKKEELERLKKRLTGLTPEKL---------EKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIE----- 429

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  723 aearhrELRALESQCQQQTQLIevltaekgqqgvgppTDNEARELaaqlalsqaqLEVHQGEVQRLQAQVVDLQAKMRAA 802
Cdd:PRK03918  430 ------ELKKAKGKCPVCGREL---------------TEEHRKEL----------LEEYTAELKRIEKELKEIEEKERKL 478

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  803 LDDQDKVQSQLSMAEAVLREHKTLvQQLKEQNEALNRAHVQELlqcsEREGALQEERADEAQQREEELRALQEELSQAK- 881
Cdd:PRK03918  479 RKELRELEKVLKKESELIKLKELA-EQLKELEEKLKKYNLEEL----EKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEe 553

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  882 CSSEEAQLEHA--ELQEQLHRANTDTAELGIQvcalTVE--KERVEEaLACAVQELQDAKEAASREREGLERqvagLQQE 957
Cdd:PRK03918  554 LKKKLAELEKKldELEEELAELLKELEELGFE----SVEelEERLKE-LEPFYNEYLELKDAEKELEREEKE----LKKL 624

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  958 KESLQEKLKAAKAAAGSLPGLQAQLAQAEQRaqsLQEAAHQELNTLKFQLSAEIMDYQSRLKNAGEECKSLRGQLEEQGR 1037
Cdd:PRK03918  625 EEELDKAFEELAETEKRLEELRKELEELEKK---YSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKE 701

                         650
                  ....*....|...
gi 157738667 1038 QLQAAEEAVEKLK 1050
Cdd:PRK03918  702 ELEEREKAKKELE 714
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 762-1098 2.87e-10

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: 65.36  E-value: 2.87e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  762 NEARELAAQLAlsqaQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNEALNRah 841
Cdd:COG3096   278 NERRELSERAL----ELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLNLVQTALRQQEKIER-- 351

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  842 vqellqcseregalqeeradeaqqREEELRALQEELSQAKCSSEEAQLEHAELQEQLHRANTDTAELGIQVC----ALTV 917
Cdd:COG3096   352 ------------------------YQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLAdyqqALDV 407

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  918 EKER----------VEEALAC-------------------------------AVQELQDAKEAASREREGLE--RQVAG- 953
Cdd:COG3096   408 QQTRaiqyqqavqaLEKARALcglpdltpenaedylaafrakeqqateevleLEQKLSVADAARRQFEKAYElvCKIAGe 487

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  954 ------LQQEKESLqEKLKAAKAAAGSLPGLQAQLAQAEQRAQSLQEA----------------AHQELNTLKFQLSAEI 1011
Cdd:COG3096   488 versqaWQTARELL-RRYRSQQALAQRLQQLRAQLAELEQRLRQQQNAerlleefcqrigqqldAAEELEELLAELEAQL 566

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667 1012 MDYQSRLKNAGE---ECKSLRGQLEEQGRQLQAAEEAVEKLKATQADMGEKLSCTSNHLAECQAAM---LRKDKEGAALR 1085
Cdd:COG3096   567 EELEEQAAEAVEqrsELRQQLEQLRARIKELAARAPAWLAAQDALERLREQSGEALADSQEVTAAMqqlLEREREATVER 646

                         410
                  ....*....|...
gi 157738667 1086 EDLERTQKELEKA 1098
Cdd:COG3096   647 DELAARKQALESQ 659
FYVE_ZFY26 cd15724
FYVE domain found in FYVE domain-containing protein 26 (ZFY26 or ZFYVE26); ZFY26, also termed ...
 1170-1228 3.48e-10

FYVE domain found in FYVE domain-containing protein 26 (ZFY26 or ZFYVE26); ZFY26, also termed FYVE domain-containing centrosomal protein (FYVE-CENT), or spastizin, is a phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) binding protein that localizes to the centrosome and midbody. ZFY26 and its interacting partners TTC19 and KIF13A are required for cytokinesis. It also interacts with Beclin 1, a subunit of class III phosphatidylinositol 3-kinase complex, and may have potential implications for carcinogenesis. In addition, it has been considered as the causal agent of a rare form of hereditary spastic paraplegia. ZFY26 contains a FYVE domain that is important for targeting of FYVE-CENT to the midbody.


Pssm-ID: 277263 [Multi-domain]  Cd Length: 61  Bit Score: 57.14  E-value: 3.48e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157738667 1170 WLGDTEANHCLDCKRE-FSWMVRRHHCRICGRIFCYYCCNNYVL-SKHGGKKERCCRACFQ 1228
Cdd:cd15724     1 WVPDEAVSVCMVCQVErFSMFNRRHHCRRCGRVVCSSCSTKKMLvEGYRENPVRVCDQCYE 61
FYVE_PKHF2 cd15755
FYVE domain found in protein containing both PH and FYVE domains 2 (phafin-2) and similar ...
 1170-1230 4.59e-10

FYVE domain found in protein containing both PH and FYVE domains 2 (phafin-2) and similar proteins; Phafin-2, also termed endoplasmic reticulum-associated apoptosis-involved protein containing PH and FYVE domains (EAPF), or pleckstrin homology domain-containing family F member 2 (PKHF2), or PH domain-containing family F member 2, or PH and FYVE domain-containing protein 2, or zinc finger FYVE domain-containing protein 18, is a ubiquitously expressed endoplasmic reticulum-associated protein that facilitates tumor necrosis factor alpha (TNF-alpha)-triggered cellular apoptosis through endoplasmic reticulum (ER)-mitochondrial apoptotic pathway. It is an endosomal phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) effector, as well as an interactor of the endosomal-tethering protein EEA1. It regulates endosome fusion upstream of Rab5. Phafin-2 also functions as a novel regulator of endocytic epidermal growth factor receptor (EGFR) degradation through a role in endosomal fusion.


Pssm-ID: 277294 [Multi-domain]  Cd Length: 64  Bit Score: 56.97  E-value: 4.59e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157738667 1170 WLGDTEANHCLDCKR-EFSWMVRRHHCRICGRIFCYYCC-NNYVLSKHGGKKERCCRACFQKL 1230
Cdd:cd15755     2 WVPDSEATVCMRCQKaKFTPVNRRHHCRKCGFVVCGPCSeKKFLLPSQSSKPVRVCDFCYDLL 64
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
611-1105 4.67e-10

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 64.40  E-value: 4.67e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  611 EEELRQANRELEKE----LQNVVGRNQLLEGKLQALQ---ADYQALQQRESAIQGSLASLEAEQASIRHLGDQMEA--SL 681
Cdd:COG4717    48 LERLEKEADELFKPqgrkPELNLKELKELEEELKEAEekeEEYAELQEELEELEEELEELEAELEELREELEKLEKllQL 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  682 LAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEVEQCQQLAEarhrELRALESQCQQQTQLIEVLTAEKGQQgvgppTD 761
Cdd:COG4717   128 LPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEA----ELAELQEELEELLEQLSLATEEELQD-----LA 198

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  762 NEARELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAAlDDQDKVQSQLSMAEAVLRehkTLVQQLKEQNEALNRAH 841
Cdd:COG4717   199 EELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAA-ALEERLKEARLLLLIAAA---LLALLGLGGSLLSLILT 274

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  842 VQELLQcseregALQEERADEAQQREEELRALQEELSQAKCSSEEAQLEHAELQEQLhrantdtAELGIqvcALTVEKER 921
Cdd:COG4717   275 IAGVLF------LVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELL-------AALGL---PPDLSPEE 338

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  922 VEEALAcAVQELQDAKEAASREREglERQVAGLQQEKESLQEKLKAAKAaagslpglqAQLAQAEQRAQSLQEAAhQELN 1001
Cdd:COG4717   339 LLELLD-RIEELQELLREAEELEE--ELQLEELEQEIAALLAEAGVEDE---------EELRAALEQAEEYQELK-EELE 405

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667 1002 TLKFQLSAEIMDYQSRLKNAGEEckSLRGQLEEQGRQLQAAEEAVEKLKATQADMGEKLSctsnhlaecqaaMLRKDKEG 1081
Cdd:COG4717   406 ELEEQLEELLGELEELLEALDEE--ELEEELEELEEELEELEEELEELREELAELEAELE------------QLEEDGEL 471

                         490       500
                  ....*....|....*....|....
gi 157738667 1082 AALREDLERTQKELEKATTKIQEY 1105
Cdd:COG4717   472 AELLQELEELKAELRELAEEWAAL 495
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 392-1168 8.71e-10

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


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 63.84  E-value: 8.71e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   392 IPSDAAQEMQELGEKLQALERERTKVEEVNRQQSAQLEQLVKELQLKEDARASLE--------RLVKEMAPLQEELSGKG 463
Cdd:pfam02463  157 EIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEyyqlkeklELEEEYLLYLDYLKLNE 236

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   464 QEADQLWRRLQELLAHTSSWEEELAELRREKKQQQEEKELLEQEVRSLTRQLQFLETQLAQVSQHVSDLEEQKKQLIQDK 543
Cdd:pfam02463  237 ERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKL 316

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   544 DHLSQQVGMLERLagppgpelpvagEKNEALVPVNSSLQEAWGKPEEEQRGLQEAQLDDTKVQEGSQEEELRQANRELEK 623
Cdd:pfam02463  317 KESEKEKKKAEKE------------LKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESE 384

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   624 ELQNVVGRNQLLEGKLQALQADYQALQQRESAIQGSLASLEAEQASIR----------HLGDQMEASLLAVRKAKEAMKA 693
Cdd:pfam02463  385 RLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILeeeeesielkQGKLTEEKEELEKQELKLLKDE 464

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   694 QMAEKEAILQSKEGECQQLREEVEQC--QQLAEARHRELRALESQCQQQTQLIEVLTAEKGQQGVGPPTDNEARELAAQL 771
Cdd:pfam02463  465 LELKKSEDLLKETQLVKLQEQLELLLsrQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVA 544

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   772 ALSQAQLEVHQGEVQRLQAQVvdLQAKMRAALDDQDKVQSQLSMAEAVLREHKTLvqqlkEQNEALNRAHVQELLQCSER 851
Cdd:pfam02463  545 ISTAVIVEVSATADEVEERQK--LVRALTELPLGARKLRLLIPKLKLPLKSIAVL-----EIDPILNLAQLDKATLEADE 617

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   852 EGALQEERADeaqQREEELRALQEELSQAKCSSEEAQLEHAELQEQLHRANTDTAELGIQVCALTVEKERVEEALACAVQ 931
Cdd:pfam02463  618 DDKRAKVVEG---ILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEI 694

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   932 ELQDAKEAASREREGLERQVAGLQQEKESLQEKLKAAKAAAGSLPGLQAQLAQAEQRAQSLQEAAHQELNTLKFQLSAEI 1011
Cdd:pfam02463  695 LRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEK 774

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  1012 MDYQSRLKNageECKSLRGQLEEQGRQLQAAEEAVEKLKATQADMGEKLsctsnhLAECQAAMLRKDKEGAALREDLERT 1091
Cdd:pfam02463  775 ELAEEREKT---EKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEE------QLLIEQEEKIKEEELEELALELKEE 845

                          730       740       750       760       770       780       790
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157738667  1092 QKELEKATTKIQEYYNKLCQEVTNRERNDQKMLADLDDLNRTKKYLEERLIELLRDKDALWQKSDALEFQQKLSAEE 1168
Cdd:pfam02463  846 QKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEER 922
FYVE_FGD6 cd15743
FYVE domain found in FYVE, RhoGEF and PH domain-containing protein 6 (FGD6) and similar ...
 1170-1227 9.60e-10

FYVE domain found in FYVE, RhoGEF and PH domain-containing protein 6 (FGD6) and similar proteins; FGD6, also termed zinc finger FYVE domain-containing protein 24 is a putative Cdc42-specific guanine nucleotide exchange factor (GEF) whose biological function remains unclear. It is a homologue of FGD1 and contains a DBL homology (DH) domain and pleckstrin homology (PH) domain in the middle region, a FYVE domain, and another PH domain in the C-terminus, but lacks the N-terminal proline-rich domain (PRD) found in FGD1. Moreover, the FYVE domain of FGD6 is a canonical FYVE domain, which has been found in many proteins involved in membrane trafficking and phosphoinositide metabolism, and has been defined by three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCR patch, and a C-terminal RVC motif, which form a compact phosphatidylinositol 3-phosphate (PtdIns3P or PI3P)-binding site.


Pssm-ID: 277282 [Multi-domain]  Cd Length: 61  Bit Score: 55.91  E-value: 9.60e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 157738667 1170 WLGDTEANHCLDCKREFSWMVRRHHCRICGRIFCYYCCNN-YVLSKHGGKKERCCRACF 1227
Cdd:cd15743     3 WIPDSRVTMCMICTSEFTVTWRRHHCRACGKVVCGSCSSNkAPLEYLKNKSARVCDECF 61
FYVE_FGD1_2_4 cd15741
FYVE domain found in FYVE, RhoGEF and PH domain-containing protein facio-genital dysplasia ...
 1169-1230 1.47e-09

FYVE domain found in FYVE, RhoGEF and PH domain-containing protein facio-genital dysplasia FGD1, FGD2, FGD4; This family represents a group of Rho GTPase cell division cycle 42 (Cdc42)-specific guanine nucleotide exchange factors (GEFs), including FYVE, RhoGEF and PH domain-containing protein FGD1, FGD2 and FGD4. FGD1, also termed faciogenital dysplasia 1 protein, or Rho/Rac guanine nucleotide exchange factor FGD1 (Rho/Rac GEF), or zinc finger FYVE domain-containing protein 3, is a central regulator of extracellular matrix remodeling and belongs to the DBL family of GEFs that regulate the activation of the Rho GTPases. FGD1 is encoded by gene FGD1. Disabling mutations in the FGD1 gene cause the human X-linked developmental disorder faciogenital dysplasia (FGDY, also known as Aarskog-Scott syndrome). FGD2, also termed zinc finger FYVE domain-containing protein 4, is expressed in antigen-presenting cells, including B lymphocytes, macrophages, and dendritic cells. It localizes to early endosomes and active membrane ruffles. It plays a role in leukocyte signaling and vesicle trafficking in cells specialized to present antigen in the immune system. FGD4, also termed actin filament-binding protein frabin, or FGD1-related F-actin-binding protein, or zinc finger FYVE domain-containing protein 6, functions as an F-actin-binding (FAB) protein showing significant homology to FGD1. It induces the formation of filopodia through the activation of Cdc42 in fibroblasts. Those FGD proteins possess a similar domain organization that contains a DBL homology (DH) domain, a pleckstrin homology (PH) domain, a FYVE domain, and another PH domain in the C-terminus. However, each FGD has a unique N-terminal region that may directly or indirectly interact with F-actin. FGD1 and FGD4 have an N-terminal proline-rich domain (PRD) and an N-terminal F-actin binding (FAB) domain, respectively. This model corresponds to the FYVE domain, which has been found in many proteins involved in membrane trafficking and phosphoinositide metabolism, and has been defined by three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCR patch, and a C-terminal RVC motif, which form a compact phosphatidylinositol 3-phosphate (PtdIns3P or PI3P)-binding site. FGD1 possesses a FYVE-like domain that lack the N-terminal WxxD motif. Moreover, FGD2 is the only known RhoGEF family member shown to have a functional FYVE domain and endosomal binding activity.


Pssm-ID: 277280 [Multi-domain]  Cd Length: 65  Bit Score: 55.57  E-value: 1.47e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157738667 1169 RWLGDTEANHCLDCKREFSWMV-RRHHCRICGRIFCYYCCNNYV-LSKHGGKKERCCRACFQKL 1230
Cdd:cd15741     2 RWVRDNEVTMCMRCKEPFNALTrRRHHCRACGYVVCWKCSDYKAtLEYDGNKLNRVCKHCYVIL 65
FYVE_ANFY1 cd15728
FYVE domain found in ankyrin repeat and FYVE domain-containing protein 1 (ANFY1) and similar ...
 1167-1230 1.65e-09

FYVE domain found in ankyrin repeat and FYVE domain-containing protein 1 (ANFY1) and similar proteins; ANFY1, also termed ankyrin repeats hooked to a zinc finger motif (Ankhzn), is a novel cytoplasmic protein that belongs to a new group of double zinc finger proteins involved in vesicle or protein transport. It is ubiquitously expressed in a spatiotemporal-specific manner and is located on endosomes. ANFY1 contains an N-terminal coiled-coil region and a BTB/POZ domain, ankyrin repeats in the middle, and a C-terminal FYVE domain.


Pssm-ID: 277267 [Multi-domain]  Cd Length: 63  Bit Score: 55.12  E-value: 1.65e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157738667 1167 EERWlgdTEANHCLDCKREFSWMVRRHHCRICGRIFCYYC-CNNYVLSKHG-GKKERCCRACFQKL 1230
Cdd:cd15728     1 EPPW---ADGDYCYECGVKFGITTRKHHCRHCGRLLCSKCsTKEVPIIKFDlNKPVRVCDVCFDVL 63
FYVE_WDFY3 cd15719
FYVE domain found in WD40 repeat and FYVE domain-containing protein 3 (WDFY3) and similar ...
 1170-1230 2.17e-09

FYVE domain found in WD40 repeat and FYVE domain-containing protein 3 (WDFY3) and similar proteins; WDFY3, also termed autophagy-linked FYVE protein (Alfy), is a ubiquitously expressed phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) binding protein required for selective macroautophagic degradation of aggregated proteins. It regulates the protein degradation through the direct interaction with the autophagy protein Atg5. Moreover, WDFY3 acts as a scaffold that bridges its cargo to the macroautophagic machinery via the creation of a greater complex with Atg12, Atg16L, and LC3. It also functionally associates with sequestosome-1/p62 (SQSTM1) in osteoclasts. WDFY3 shuttles between the nucleus and cytoplasm. It predominantly localizes to the nucleus and nuclear membrane under basal conditions, but is recruited to cytoplasmic ubiquitin-positive protein aggregates under stress conditions. WDFY3 contains a PH-BEACH domain assemblage, five WD40 repeats and a PtdIns3P-binding FYVE domain.


Pssm-ID: 277259 [Multi-domain]  Cd Length: 65  Bit Score: 55.08  E-value: 2.17e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157738667 1170 WLGDTEANHCLDCKREFSWMVRRHHCRICGRIFCYYCCNN--YVLSKHGGKKERCCRACFQKL 1230
Cdd:cd15719     3 WVKDEGGDSCTGCSVRFSLTERRHHCRNCGQLFCSKCSRFesEIRRLRISRPVRVCQACYNIL 65
mukB PRK04863
chromosome partition protein MukB;
511-1164 2.34e-09

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 62.28  E-value: 2.34e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  511 LTRQLQFLETQLAQVSQH---VSDLEEQKKQLIQDKDHLsqqvgmlerlagppgpelpvaGEKNEALVPVNSSLQEAWGK 587
Cdd:PRK04863  319 LNEAESDLEQDYQAASDHlnlVQTALRQQEKIERYQADL---------------------EELEERLEEQNEVVEEADEQ 377

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  588 PEEEQRGLQEAQL--DDTK-----VQEGSQEEELR-----QANRELEK----------ELQNVVGRNQLLEGKLQALQAD 645
Cdd:PRK04863  378 QEENEARAEAAEEevDELKsqladYQQALDVQQTRaiqyqQAVQALERakqlcglpdlTADNAEDWLEEFQAKEQEATEE 457

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  646 YQALQQRESAIQGSLASLEAEQASIRHLGDQMEASlLAVRKAKEAmkaqmaekeailqskegeCQQLREEVEQCQQLaEA 725
Cdd:PRK04863  458 LLSLEQKLSVAQAAHSQFEQAYQLVRKIAGEVSRS-EAWDVAREL------------------LRRLREQRHLAEQL-QQ 517

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  726 RHRELRALESQCQQQTQLIEVLTAEKGQQGVGPPTDNEARELAAQLalsQAQLEVHQGEvqrlQAQVVDLQAKMRAALDD 805
Cdd:PRK04863  518 LRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEEL---EARLESLSES----VSEARERRMALRQQLEQ 590

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  806 QDKVQSQLSMAEAVLREHKTLVQQLKEQNEA--LNRAHVQELLQ-CSEREGALQEERaDEAQQREEELRALQEELSQAKc 882
Cdd:PRK04863  591 LQARIQRLAARAPAWLAAQDALARLREQSGEefEDSQDVTEYMQqLLERERELTVER-DELAARKQALDEEIERLSQPG- 668

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  883 SSEEAQLEH----------AELQE--QLHRANTDTAELGIQVCALTV-EKERVEEALA----C----------------- 928
Cdd:PRK04863  669 GSEDPRLNAlaerfggvllSEIYDdvSLEDAPYFSALYGPARHAIVVpDLSDAAEQLAgledCpedlyliegdpdsfdds 748

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  929 --AVQELQDA--KEAASRE-------------REGLERQVAGLQQEKESLQEKLkaakaaagslpglqAQLAQAEQRAQS 991
Cdd:PRK04863  749 vfSVEELEKAvvVKIADRQwrysrfpevplfgRAAREKRIEQLRAEREELAERY--------------ATLSFDVQKLQR 814

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  992 LQEAAHQELNT---LKFQL--SAEIMDYQSRLKNAGEECKSLRGQLEEQGRQLQAAEEAVEKLKATQADM--------GE 1058
Cdd:PRK04863  815 LHQAFSRFIGShlaVAFEAdpEAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSALNRLLPRLnlladetlAD 894

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667 1059 KLSCTSNHLAECQAAMLRKDKEGAALR-------------EDLERTQKELEKATTKIQEYYNK---LCQEVTNRE----R 1118
Cdd:PRK04863  895 RVEEIREQLDEAEEAKRFVQQHGNALAqlepivsvlqsdpEQFEQLKQDYQQAQQTQRDAKQQafaLTEVVQRRAhfsyE 974

                         730       740       750       760       770
                  ....*....|....*....|....*....|....*....|....*....|.
gi 157738667 1119 NDQKMLADLDDLN-RTKKYLEERLIELLRDKDALWQK----SDALEFQQKL 1164
Cdd:PRK04863  975 DAAEMLAKNSDLNeKLRQRLEQAEQERTRAREQLRQAqaqlAQYNQVLASL 1025
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
596-1104 2.66e-09

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 61.98  E-value: 2.66e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  596 QEAQLDDTKVQ-EGSQEEELRQANRELEKELQNVVGRNQLLEGKLQALQADYQALQQRESAIQGSLASLEAEQASIRHLg 674
Cdd:PRK02224  185 QRGSLDQLKAQiEEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDL- 263

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  675 dqmEASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEVE---QCQQLAEARHRELRALESQCQQQTQLIEVLTAEK 751
Cdd:PRK02224  264 ---RETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGlddADAEAVEARREELEDRDEELRDRLEECRVAAQAH 340

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  752 GQQGVGPPTD------------NEARELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLsmaEAV 819
Cdd:PRK02224  341 NEEAESLREDaddleeraeelrEEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFL---EEL 417

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  820 LREHKTLVQQLKE-----QNEALNRAHVQELL---QCSEREGALQE-ERADEAQQREEELRALQEELsqakcssEEAQLE 890
Cdd:PRK02224  418 REERDELREREAEleatlRTARERVEEAEALLeagKCPECGQPVEGsPHVETIEEDRERVEELEAEL-------EDLEEE 490

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  891 HAELQEQLHRAnTDTAELGIQVCALTVEKERVEEALACAVQELQDAKEAASREREGLERQVAGLQQEKESLQEKLKAAKA 970
Cdd:PRK02224  491 VEEVEERLERA-EDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEE 569

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  971 AAGSLPGLQAQLAQAEQRAQSLqeaahqelntlkfqlsAEIMDYQSRLKNAGEECKSLRGQLEEQGRQLQAAEEAVEKLK 1050
Cdd:PRK02224  570 AREEVAELNSKLAELKERIESL----------------ERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKR 633

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....
gi 157738667 1051 ATQADMGEKLSctsnhlaecqaamlrkDKEGAALREDLERTQKELEKATTKIQE 1104
Cdd:PRK02224  634 ERKRELEAEFD----------------EARIEEAREDKERAEEYLEQVEEKLDE 671
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 590-956 4.03e-09

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: 61.51  E-value: 4.03e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  590 EEQRGLQEAQLDDTKVQEGSQEE--ELRQANRELEKELQNVVGRNQLLEGKLQA----LQADYQALQQRESaiqgslasL 663
Cdd:COG3096   278 NERRELSERALELRRELFGARRQlaEEQYRLVEMARELEELSARESDLEQDYQAasdhLNLVQTALRQQEK--------I 349

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  664 EAEQASIRHLGDQMEASLLAVRKAKEamkaQMAEKEAILQSKEGECQQLREEVEQCQQLAEARHRE-------LRALEsQ 736
Cdd:COG3096   350 ERYQEDLEELTERLEEQEEVVEEAAE----QLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQTRaiqyqqaVQALE-K 424

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  737 CQQQTQLIEvLTAE-----------KGQQGvgpptDNEARELAAQLALSQAQLEVHQ----------GEVQRLQA----- 790
Cdd:COG3096   425 ARALCGLPD-LTPEnaedylaafraKEQQA-----TEEVLELEQKLSVADAARRQFEkayelvckiaGEVERSQAwqtar 498

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  791 QVVDLQAKMRAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNEALNR-------------AHVQELLQCSEREGALQE 857
Cdd:COG3096   499 ELLRRYRSQQALAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQqldaaeeleellaELEAQLEELEEQAAEAVE 578

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  858 ERAdEAQQREEELRALQEELSQAKCSSEEAQLEHAELQEQLHRANTDTAELgIQVCALTVEKERveealacavqELQDAK 937
Cdd:COG3096   579 QRS-ELRQQLEQLRARIKELAARAPAWLAAQDALERLREQSGEALADSQEV-TAAMQQLLERER----------EATVER 646

                         410
                  ....*....|....*....
gi 157738667  938 EAASREREGLERQVAGLQQ 956
Cdd:COG3096   647 DELAARKQALESQIERLSQ 665
FYVE_spVPS27p_like cd15735
FYVE domain found in Schizosaccharomyces pombe vacuolar protein sorting-associated protein 27 ...
 1174-1227 4.87e-09

FYVE domain found in Schizosaccharomyces pombe vacuolar protein sorting-associated protein 27 (spVps27p) and similar proteins; spVps27p, also termed suppressor of ste12 deletion protein 4 (Sst4p), is a conserved homolog of budding Saccharomyces cerevisiae Vps27 and of mammalian Hrs. It functions as a downstream factor for phosphatidylinositol 3-kinase (PtdIns 3-kinase) in forespore membrane formation with normal morphology. It colocalizes and interacts with Hse1p, a homolog of Saccharomyces cerevisiae Hse1p and of mammalian STAM, to form a complex whose ubiquitin-interacting motifs (UIMs) are important for sporulation. spVps27p contains a VHS (Vps27p/Hrs/Stam) domain, a FYVE domain, and two UIMs.


Pssm-ID: 277274 [Multi-domain]  Cd Length: 59  Bit Score: 53.69  E-value: 4.87e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 157738667 1174 TEANHCLDCKREFSWMVRRHHCRICGRIFCYYCCNNYVLSKHGGKKE--RCCRACF 1227
Cdd:cd15735     4 VDSDVCMRCRTAFTFTNRKHHCRNCGGVFCQQCSSKSLPLPHFGINQpvRVCDGCY 59
FYVE_ZFY19 cd15749
FYVE-related domain found in FYVE domain-containing protein 19 (ZFY19) and similar proteins; ...
 1179-1227 5.15e-09

FYVE-related domain found in FYVE domain-containing protein 19 (ZFY19) and similar proteins; ZFY19, also termed mixed lineage leukemia (MLL) partner containing FYVE domain, is encoded by a novel gene, MLL partner containing FYVE domain (MPFYVE). The FYVE domain of ZFY19 resembles FYVE-related domains that are structurally similar to the canonical FYVE domains but lack the three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif. The biological function of ZFY19 remains unclear.


Pssm-ID: 277288 [Multi-domain]  Cd Length: 51  Bit Score: 53.28  E-value: 5.15e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 157738667 1179 CLDCKREFSWMVRRHHCRICGRIFCYYCCN-NYVLSKHGGKKERCCRACF 1227
Cdd:cd15749     2 CFGCAAKFSLFKKECGCKNCGRSFCKGCLTfSAVVPRKGNQKQKVCKQCH 51
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
767-994 6.09e-09

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 60.80  E-value: 6.09e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  767 LAAQLALSQAQLEVHQGEVQRLQAQ--VVDLQAKMRAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNeALNRAHVQE 844
Cdd:COG3206   180 LEEQLPELRKELEEAEAALEEFRQKngLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQL-GSGPDALPE 258

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  845 LLQcSEREGALQEERADEAQQREEELRALQEELSQAKcsseeaqlehaELQEQLhrantdtaelgiqvcaltvekERVEE 924
Cdd:COG3206   259 LLQ-SPVIQQLRAQLAELEAELAELSARYTPNHPDVI-----------ALRAQI---------------------AALRA 305

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  925 ALAcavQELQDAKEAASREREGLERQVAGLQQEKESLQEKLKaakaaagSLPGLQAQLAQAEQRAQSLQE 994
Cdd:COG3206   306 QLQ---QEAQRILASLEAELEALQAREASLQAQLAQLEARLA-------ELPELEAELRRLEREVEVARE 365
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 720-964 1.05e-08

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: 59.01  E-value: 1.05e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  720 QQLAEARHRELRALESQCQQQTQLIEVLTAEKgqqgvgpptdneaRELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKM 799
Cdd:COG4942    19 ADAAAEAEAELEQLQQEIAELEKELAALKKEE-------------KALLKQLAALERRIAALARRIRALEQELAALEAEL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  800 RAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNEALNRAHVQELLQcSEREGALQEERADEAQQREEELRALQEELSQ 879
Cdd:COG4942    86 AELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLD-AVRRLQYLKYLAPARREQAEELRADLAELAA 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  880 AKcssEEAQLEHAELQEQLHRANTDTAELGiqvcALTVEKERVEEALACAVQELQDAKEAASREREGLERQVAGLQQEKE 959
Cdd:COG4942   165 LR---AELEAERAELEALLAELEEERAALE----ALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237


                  ....*
gi 157738667  960 SLQEK 964
Cdd:COG4942   238 AAAER 242
RUN_RUNDC3A cd17699
RUN domain found in RUN domain-containing protein 3A (RUNDC3A) and similar proteins; RUN ...
 33-162 1.07e-08

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: 55.80  E-value: 1.07e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   33 EPITDDSTSLHKFSYKLEYLLQFDQKEKATLLGN--KKDYWDYFCACLAKVkgANDGIRFVKSISELRTSLGKGRAFIRY 110
Cdd:cd17699    20 EPIDDSSEEFVNFAAILEQILSHRFKGPVSWFSSdgQRGFWDYIRLACSKV--PNNCISSIENMENISTSRAKGRAWIRV 97

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 157738667  111 SLVHQRLADTLQQCFMNTKVTSDWYYARSPFLQPKlSSDIVGQLYELTEVQF 162
Cdd:cd17699    98 ALMEKRLSEYIATALRDTRTTRRFYDDGAIMLREE-STVLTGMLIGLSAIDF 148
mukB PRK04863
chromosome partition protein MukB;
234-965 1.07e-08

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 60.36  E-value: 1.07e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  234 EMRLELDQLEVREKQLRERMQQLDRENQELRAAVSQQG--EQLQTERERGRTAAEDNVRLTCLVAELQKQWEV-TQATQN 310
Cdd:PRK04863  311 EMARELAELNEAESDLEQDYQAASDHLNLVQTALRQQEkiERYQADLEELEERLEEQNEVVEEADEQQEENEArAEAAEE 390

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  311 TVKELQTCL----QGLELgAAEKEEDYHTALRRLESM-----LQPLAQE-LEATRDSLDKKNQHLASFpgwLAMAQQKAD 380
Cdd:PRK04863  391 EVDELKSQLadyqQALDV-QQTRAIQYQQAVQALERAkqlcgLPDLTADnAEDWLEEFQAKEQEATEE---LLSLEQKLS 466

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  381 TASDTKGRQE-----------PI-PSDAAQEMQEL----------GEKLQALERERTKVEEVNRQQsAQLEQLVKEL--- 435
Cdd:PRK04863  467 VAQAAHSQFEqayqlvrkiagEVsRSEAWDVARELlrrlreqrhlAEQLQQLRMRLSELEQRLRQQ-QRAERLLAEFckr 545

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  436 ------------QLKEDARASLERLVKEMAPLQEELSGKGQEADQLWRRLQELLAHTSSWEEELAelrrekkqqqeekel 503
Cdd:PRK04863  546 lgknlddedeleQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAWLAAQD--------------- 610

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  504 leqevrSLTR-QLQFLETQL--AQVSQHVSDLEEQKKQLIQDKDHLSQQVGML----ERLAGPPGPELPVAGEKNEALVP 576
Cdd:PRK04863  611 ------ALARlREQSGEEFEdsQDVTEYMQQLLERERELTVERDELAARKQALdeeiERLSQPGGSEDPRLNALAERFGG 684

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  577 VnsSLQEAWgkpeeeqrglqeaqlDDTKVQEGSQEE----ELRQA--NRELEKELQNVVGRNQLLEgKLQALQADYQALQ 650
Cdd:PRK04863  685 V--LLSEIY---------------DDVSLEDAPYFSalygPARHAivVPDLSDAAEQLAGLEDCPE-DLYLIEGDPDSFD 746

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  651 QresaiqGSLASLEAEQASIRHLGD-QMEAS------LLAvRKAKEAmkaQMAEKEAILQSKEGECQQLREEVEQCQQLA 723
Cdd:PRK04863  747 D------SVFSVEELEKAVVVKIADrQWRYSrfpevpLFG-RAAREK---RIEQLRAEREELAERYATLSFDVQKLQRLH 816

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  724 EA------------------------------RHRELRALESQCQQQTQLIEvlTAEKGQQGVG-----------PPTDN 762
Cdd:PRK04863  817 QAfsrfigshlavafeadpeaelrqlnrrrveLERALADHESQEQQQRSQLE--QAKEGLSALNrllprlnlladETLAD 894

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  763 EARELAAQLA-LSQAQLEVHQGevQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNEalNRAH 841
Cdd:PRK04863  895 RVEEIREQLDeAEEAKRFVQQH--GNALAQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQ--RRAH 970

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  842 ------VQELLQCSEREGALQEERADEAQQRE---EELRALQEELSQAKCSSEEAQLEHAELQEQLHRANTDTAELGIQV 912
Cdd:PRK04863  971 fsyedaAEMLAKNSDLNEKLRQRLEQAEQERTrarEQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDLGVPA 1050

                         810       820       830       840       850
                  ....*....|....*....|....*....|....*....|....*....|...
gi 157738667  913 CaltvekERVEEALACAVQELQDAKEAASREREGLERQVAGLQQEKESLQEKL 965
Cdd:PRK04863 1051 D------SGAEERARARRDELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKL 1097
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 234-898 1.34e-08

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 59.60  E-value: 1.34e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   234 EMRLELDQLEVREKQLRERMQQLDRENQELRAAVSQQgEQLQTERERGRTAAEDNVRLTCLVAELQKQWEVTQATQNTVK 313
Cdd:TIGR00618  202 RSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQT-QQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLE 280

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   314 ELQTCLQglELGAAEKEEDYHTALRRLESMLQPLAQELEATRDSLDKKNQHLAsfpgwlAMAQQKADTASDTKgrqepip 393
Cdd:TIGR00618  281 ETQERIN--RARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRA------AHVKQQSSIEEQRR------- 345

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   394 sdAAQEMQELGEKLQALERERTKVEEVNRQQSAQLEQLVKELQLKEDARASLERLVKEMAPLQEElSGKGQEADQLWRRL 473
Cdd:TIGR00618  346 --LLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQRE-QATIDTRTSAFRDL 422

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   474 QELLAHTSSWEEELAELRREKKQ----QQEEKELLEQEVRSLTRQLQFLETQLAQVSQHVSDLEEQKKQLIQDKDHLSQQ 549
Cdd:TIGR00618  423 QGQLAHAKKQQELQQRYAELCAAaitcTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEE 502

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   550 VGMLERLAGPPGPELPVAGEKNEALVPV---------------------NSSLQEAWGKPEEEQRGLQEAQLDDTKVQEG 608
Cdd:TIGR00618  503 PCPLCGSCIHPNPARQDIDNPGPLTRRMqrgeqtyaqletseedvyhqlTSERKQRASLKEQMQEIQQSFSILTQCDNRS 582

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   609 SQE--------EELRQANRELEKELQNVVGRNQLLEGKLQALQADYQA---LQQRESAIQGSLASLEAEQASIrhLGDQM 677
Cdd:TIGR00618  583 KEDipnlqnitVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVrlhLQQCSQELALKLTALHALQLTL--TQERV 660

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   678 EASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEVEQCQQLAEARHRELRALESQCQQQTQLievltaekgqqgvg 757
Cdd:TIGR00618  661 REHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENA-------------- 726

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   758 pptdneareLAAQLALSQAQLEVHQGEVQRLQAQvvdlqakMRAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNEAL 837
Cdd:TIGR00618  727 ---------SSSLGSDLAAREDALNQSLKELMHQ-------ARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFF 790

                          650       660       670       680       690       700
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157738667   838 NRAHVQELLQCSEREGALQEERADEAQQREEELRALQEELSQAKCSSEEAQLEHAELQEQL 898
Cdd:TIGR00618  791 NRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQL 851
PTZ00121 PTZ00121
MAEBL; Provisional
 219-965 2.40e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 59.00  E-value: 2.40e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  219 DLNSPLNNEALEGFDEMRLELDQLEVREkqlrerMQQLDRENQ-----ELRAAVSQQGEQLQTERERGRTAAEDNVRLTC 293
Cdd:PTZ00121 1019 DFNQNFNIEKIEELTEYGNNDDVLKEKD------IIDEDIDGNhegkaEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEA 1092

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  294 LVAELQKQWEVTQATQNTVKELQTCLQglelgAAEKEEDYHTA--LRRLESmlqplAQELEATRDSLDKKNQHLASfpgw 371
Cdd:PTZ00121 1093 TEEAFGKAEEAKKTETGKAEEARKAEE-----AKKKAEDARKAeeARKAED-----ARKAEEARKAEDAKRVEIAR---- 1158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  372 lamAQQKADTASDTKGRQEPIPSDAAQEMQELGEKlqaleRERTKVEEVNRQQSAQLEQLVKELqlkEDARASLERLVKE 451
Cdd:PTZ00121 1159 ---KAEDARKAEEARKAEDAKKAEAARKAEEVRKA-----EELRKAEDARKAEAARKAEEERKA---EEARKAEDAKKAE 1227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  452 MAPLQEELSGKGQEAdqlwRRLQELLAHTSSWEEELAELRREKKQQQEEKELLEQEVRSLTRQLQFLETQLAQVSQHVSD 531
Cdd:PTZ00121 1228 AVKKAEEAKKDAEEA----KKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKK 1303

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  532 LEEQKKQLIQDK--DHLSQQVGMLERLAGPPGPELPVAGEKNEAlvpvnsSLQEAWGKPEEEQRGLQEAQLDDTKVQEGS 609
Cdd:PTZ00121 1304 ADEAKKKAEEAKkaDEAKKKAEEAKKKADAAKKKAEEAKKAAEA------AKAEAEAAADEAEAAEEKAEAAEKKKEEAK 1377

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  610 QE--------EELRQANrELEKELQNVVGRNQLLEGKLQALQADYQALQQRESAIQGSLASLEAEQA----SIRHLGDQM 677
Cdd:PTZ00121 1378 KKadaakkkaEEKKKAD-EAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAkkadEAKKKAEEA 1456

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  678 EASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEV----EQCQQLAEARHR--ELRALES--------QCQQQTQL 743
Cdd:PTZ00121 1457 KKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAkkkaDEAKKAAEAKKKadEAKKAEEakkadeakKAEEAKKA 1536

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  744 IEVLTAEKGQQGVGPPTDNEARELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAVLR-- 821
Cdd:PTZ00121 1537 DEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKae 1616

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  822 EHKTLVQQLKEQNEAlnRAHVQELLQCSEREGALQEE----------RADEAQQREEELRALQEELSQA---KCSSEEAQ 888
Cdd:PTZ00121 1617 EAKIKAEELKKAEEE--KKKVEQLKKKEAEEKKKAEElkkaeeenkiKAAEEAKKAEEDKKKAEEAKKAeedEKKAAEAL 1694

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  889 LEHAELQ---EQLHRANTDTAELGIQV-CALTVEKERVEEALACAVQELQDAKEAasREREGLERQVAGLQQEKESLQEK 964
Cdd:PTZ00121 1695 KKEAEEAkkaEELKKKEAEEKKKAEELkKAEEENKIKAEEAKKEAEEDKKKAEEA--KKDEEEKKKIAHLKKEEEKKAEE 1772


                  .
gi 157738667  965 L 965
Cdd:PTZ00121 1773 I 1773
FYVE_PKHF1 cd15754
FYVE domain found in protein containing both PH and FYVE domains 1 (phafin-1) and similar ...
 1170-1230 3.01e-08

FYVE domain found in protein containing both PH and FYVE domains 1 (phafin-1) and similar proteins; Phafin-1, also termed lysosome-associated apoptosis-inducing protein containing PH (pleckstrin homology) and FYVE domains (LAPF), or pleckstrin homology domain-containing family F member 1 (PKHF1), or PH domain-containing family F member 1, or apoptosis-inducing protein, or PH and FYVE domain-containing protein 1, or zinc finger FYVE domain-containing protein 15, is a representative of a novel family of PH and FYVE domain-containing proteins called phafins. It is a ubiquitously expressed pro-apoptotic protein via translocating to lysosomes, facilitating apoptosis induction through a lysosomal-mitochondrial apoptotic pathway.


Pssm-ID: 277293 [Multi-domain]  Cd Length: 64  Bit Score: 51.88  E-value: 3.01e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157738667 1170 WLGDTEANHCLDCKR-EFSWMVRRHHCRICGRIFCYYCCN-NYVLSKHGGKKERCCRACFQKL 1230
Cdd:cd15754     2 WIPDKATDICMRCTQtNFSLLTRRHHCRKCGFVVCHECSRqRFLIPRLSPKPVRVCSLCYRKL 64
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 579-1168 3.03e-08

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


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 58.70  E-value: 3.03e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   579 SSLQEAWGKPEEEQRGL--QEAQLDDTKVQEGSQEEELRQanrELEKELQNVVGRNQLLEGKLQALQADYQALQQ-RESA 655
Cdd:pfam12128  311 SAADAAVAKDRSELEALedQHGAFLDADIETAAADQEQLP---SWQSELENLEERLKALTGKHQDVTAKYNRRRSkIKEQ 387

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   656 IQGSLASLEAEQASIRhlgdqmeasllavrkakEAMKAQMAEKEAILQskeGECQQLREEVEQcqQLAEARhrelrales 735
Cdd:pfam12128  388 NNRDIAGIKDKLAKIR-----------------EARDRQLAVAEDDLQ---ALESELREQLEA--GKLEFN--------- 436

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   736 qcQQQTQLIEVLTAEKGQQGVGPPTDnearELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSM 815
Cdd:pfam12128  437 --EEEYRLKSRLGELKLRLNQATATP----ELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQ 510

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   816 AEAVLREHKTLVQQLKEQNEAlnRAHvqELLQCSEREGALQEERADEAQQREEELRA-LQEELSQAKCSSEEA------- 887
Cdd:pfam12128  511 ASRRLEERQSALDELELQLFP--QAG--TLLHFLRKEAPDWEQSIGKVISPELLHRTdLDPEVWDGSVGGELNlygvkld 586

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   888 --QLEH---AELQEQLhRANTDTAELGIQvcALTVEKERVEEALACAVQELQDAKEAASREREGLE-------RQVAGLQ 955
Cdd:pfam12128  587 lkRIDVpewAASEEEL-RERLDKAEEALQ--SAREKQAAAEEQLVQANGELEKASREETFARTALKnarldlrRLFDEKQ 663

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   956 QEKESLQEKlkaakaaagslpgLQAQLAQAEQRAQSLQEAAHQELNTLKfQLSAEImdyqsrlknageeckslRGQLEEQ 1035
Cdd:pfam12128  664 SEKDKKNKA-------------LAERKDSANERLNSLEAQLKQLDKKHQ-AWLEEQ-----------------KEQKREA 712

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  1036 GRQLQAAEEAVEKLKATQADM--GEKLSCTSNHLAECQAAMLRKDKEGAAL-------------REDLERTQKELEKATT 1100
Cdd:pfam12128  713 RTEKQAYWQVVEGALDAQLALlkAAIAARRSGAKAELKALETWYKRDLASLgvdpdviaklkreIRTLERKIERIAVRRQ 792

                          570       580       590       600       610       620       630
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157738667  1101 KIQEYYNKLcQEVTNRERndQKMLADLDDLNRTKKYLEERLIELL----RDKDALWQKSDALEFQQKLSAEE 1168
Cdd:pfam12128  793 EVLRYFDWY-QETWLQRR--PRLATQLSNIERAISELQQQLARLIadtkLRRAKLEMERKASEKQQVRLSEN 861
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 388-1090 3.16e-08

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: 58.65  E-value: 3.16e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   388 RQEPIPSDAAQEMQELGEKLQALERERTKVEEVNRQQSAQLEQLVKELQLK-------EDARASLERLVKEMAPLQEELS 460
Cdd:pfam01576    2 RQEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAEtelcaeaEEMRARLAARKQELEEILHELE 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   461 GKGQEADQLWRRLQ----ELLAHTSSWEEELAELRREKKQQQEEKELLEQEVRSLTRQLQFLETQLAQVSQHVSDLEEQK 536
Cdd:pfam01576   82 SRLEEEEERSQQLQnekkKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERI 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   537 KQLIQDKDHLSQQVGMLERLAGPPGPELPVAGEKNEALVPVNSSLQEAWGKPEEEQRGLQE------AQLDDTKVQEGSQ 610
Cdd:pfam01576  162 SEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEqiaelqAQIAELRAQLAKK 241

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   611 EEELRQANRELEKElqnvVGRNQLLEGKLQALQADYQALQQRESAIQGSLASLEAEQasiRHLGDQMEasllAVRKAKEA 690
Cdd:pfam01576  242 EEELQAALARLEEE----TAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQR---RDLGEELE----ALKTELED 310

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   691 MKAQMAEKEAILQSKEGECQQLREEVEQ-----CQQLAEARHRELRALESQCQQQTQLIEVLTA-EKGQQGVgpptDNEA 764
Cdd:pfam01576  311 TLDTTAAQQELRSKREQEVTELKKALEEetrshEAQLQEMRQKHTQALEELTEQLEQAKRNKANlEKAKQAL----ESEN 386

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   765 RELAAQL-ALSQAQLEVHQGEvQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNEALNRAHVQ 843
Cdd:pfam01576  387 AELQAELrTLQQAKQDSEHKR-KKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSS 465

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   844 ELLQCSEREGALQEER------ADEAQQREEELRALQEELSQAKCSSEEAQLEHAELQEQLHRANTDTAELGIQVCALTV 917
Cdd:pfam01576  466 LESQLQDTQELLQEETrqklnlSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEE 545

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   918 EKERVEEALACAVQELQDAKEAASReregLERQVAGLQQEKESLQEKLKAAKAAAGSLPGLQAQLAQ--AEQRAQSLQ-- 993
Cdd:pfam01576  546 GKKRLQRELEALTQQLEEKAAAYDK----LEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQmlAEEKAISARya 621

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   994 ------EAAHQELNTLKFQLSAEIMDYQSRLKNAGEECKSLRGQLEE-------QGRQLQAAEEAVEKLKATQADMGEKL 1060
Cdd:pfam01576  622 eerdraEAEAREKETRALSLARALEEALEAKEELERTNKQLRAEMEDlvsskddVGKNVHELERSKRALEQQVEEMKTQL 701

                          730       740       750
                   ....*....|....*....|....*....|
gi 157738667  1061 SCTSNHLAECQAAMLRKDKEGAALREDLER 1090
Cdd:pfam01576  702 EELEDELQATEDAKLRLEVNMQALKAQFER 731
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
400-924 3.80e-08

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 57.86  E-value: 3.80e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  400 MQELGEKLQALERERTKVEEVNRQQSAQLEQLVKELQLKEDARASLERLVKEMAPLQEELSGKGQEADQLWRRLQELLAH 479
Cdd:COG4717    48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQL 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  480 TSSWEEElaelrrekkqqqeekelleqevRSLTRQLQFLETQLAQVSQHVSDLEEQKKQLiqdkDHLSQQVGMLERlagp 559
Cdd:COG4717   128 LPLYQEL----------------------EALEAELAELPERLEELEERLEELRELEEEL----EELEAELAELQE---- 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  560 pgpelpvagEKNEALVPVNSSLQEAWGKPEEEQrglqeaqlddtkvqegsqeEELRQANRELEKELQNVVGRNQLLEGKL 639
Cdd:COG4717   178 ---------ELEELLEQLSLATEEELQDLAEEL-------------------EELQQRLAELEEELEEAQEELEELEEEL 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  640 QALQADYQALQQRES-AIQGSLASLEAEQASIRHLGDQMEASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEVEQ 718
Cdd:COG4717   230 EQLENELEAAALEERlKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQA 309

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  719 CQQLAEARHRELRALESQCQQQTQLIEVLTAEKGQQGVgpptdnEARELAAQL--ALSQAQLEVHQGEVQRLQAQVvdlQ 796
Cdd:COG4717   310 LPALEELEEEELEELLAALGLPPDLSPEELLELLDRIE------ELQELLREAeeLEEELQLEELEQEIAALLAEA---G 380

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  797 AKMRAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNEALNRAHVQELLQcsEREGALQEERADEAQQRE---EELRAL 873
Cdd:COG4717   381 VEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELE--EELEELEEELEELEEELEelrEELAEL 458

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|...
gi 157738667  874 QEELSQAKCSSE--EAQLEHAELQEQLHRANTDTAELGIQVCALTVEKERVEE 924
Cdd:COG4717   459 EAELEQLEEDGElaELLQELEELKAELRELAEEWAALKLALELLEEAREEYRE 511
FYVE_FGD5 cd15742
FYVE-like domain found in FYVE, RhoGEF and PH domain-containing protein 5 (FGD5) and similar ...
 1179-1230 3.99e-08

FYVE-like domain found in FYVE, RhoGEF and PH domain-containing protein 5 (FGD5) and similar proteins; FGD5, also termed zinc finger FYVE domain-containing protein 23, is an endothelial cell (EC)-specific guanine nucleotide exchange factor (GEF) that regulates endothelial adhesion, survival, and angiogenesis by modulating phosphatidylinositol 3-kinase signaling. It functions as a novel genetic regulator of vascular pruning by activation of endothelial cell-targeted apoptosis. FGD5 is a homologue of FGD1 and contains a DBL homology (DH) domain, a pleckstrin homology (PH) domain, a FYVE domain, and another PH domain in the C-terminus, but lacks the N-terminal proline-rich domain (PRD) found in FGD1. The FYVE domain of FGD5 resembles a FYVE-like domain that is different from the canonical FYVE domains, since it lacks one of the three conserved signature motifs (the WxxD motif) that are involved in phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) binding and exhibits altered lipid binding specificities.


Pssm-ID: 277281 [Multi-domain]  Cd Length: 67  Bit Score: 51.47  E-value: 3.99e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 157738667 1179 CLDCKREFSWMVRRHHCRICGRIFCYYCC-NNYVLSKHGGKKERCCRACFQKL 1230
Cdd:cd15742    12 CMNCGSDFTLTLRRHHCHACGKIVCRNCSrNKYPLKYLKDRPAKVCDGCFAEL 64
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 767-1032 4.37e-08

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: 57.08  E-value: 4.37e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  767 LAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNEALNRahvqELL 846
Cdd:COG4942    11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEA----ELA 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  847 QCSEREGALQEERADEAQQREEELRALQEelsqakcSSEEAQLEHAELQEQLHRANTDTAELGiqvcALTVEKERVEEAL 926
Cdd:COG4942    87 ELEKEIAELRAELEAQKEELAELLRALYR-------LGRQPPLALLLSPEDFLDAVRRLQYLK----YLAPARREQAEEL 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  927 ACAVQELQDAKEAASREREGLERQVAGLQQEKESLQEKLKAAKAAagsLPGLQAQLAQAEQRAQSLQEAAhQELNTLKFQ 1006
Cdd:COG4942   156 RADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKL---LARLEKELAELAAELAELQQEA-EELEALIAR 231

                         250       260
                  ....*....|....*....|....*.
gi 157738667 1007 LSAEIMDYQSRLKNAGEecKSLRGQL 1032
Cdd:COG4942   232 LEAEAAAAAERTPAAGF--AALKGKL 255
FYVE_scVPS27p_Vac1p_like cd15736
FYVE domain found in Saccharomyces cerevisiae vacuolar protein sorting-associated protein 27 ...
 1179-1227 6.48e-08

FYVE domain found in Saccharomyces cerevisiae vacuolar protein sorting-associated protein 27 (scVps27p) and FYVE-related domain 1 found in yeast protein VAC1 (Vac1p) and similar proteins; The family includes Saccharomyces cerevisiae vacuolar protein sorting-associated protein 27 (scVps27p) and protein VAC1 (Vac1p). scVps27p, also termed Golgi retention defective protein 11, is the putative yeast counterpart of the mammalian protein Hrs and is involved in endosome maturation. It is a mono-ubiquitin-binding protein that interacts with ubiquitinated cargoes, such as Hse1p, and is required for protein sorting into the multivesicular body. Vps27p forms a complex with Hse1p. The complex binds ubiquitin and mediates endosomal protein sorting. At the endosome, Vps27p and a trimeric protein complex, ESCRT-1, bind ubiquitin and are important for multivesicular body (MVB) sorting. Vps27p contains an N-terminal VHS (Vps27/Hrs/STAM) domain, a FYVE domain that binds PtdIns3P, followed by two ubiquitin-interacting motifs (UIMs), and a C-terminal clathrin-binding motif. Vac1p, also termed vacuolar segregation protein Pep7p, or carboxypeptidase Y-deficient protein 7, or vacuolar protein sorting-associated protein 19 (Vps19p), or vacuolar protein-targeting protein 19, is a phosphatidylinositol 3-phosphate (PtdIns3P or PI3P)-binding protein that interacts with a Rab GTPase, GTP-bound form of Vps21p, and a Sec1p homologue, Vps45p, to facilitate Vps45p-dependent vesicle-mediated vacuolar protein sorting. It also acts as a novel regulator of vesicle docking and/or fusion at the endosome and functions in vesicle-mediated transport of Golgi precursor carboxypeptidase Y (CPY), protease A (PrA), protease B (PrB), but not alkaline phosphatase (ALP) from the trans-Golgi network-like compartment (TGN) to the endosome. Vac1p contains an N-terminal classical TFIIIA-like zinc finger, two putative zinc-binding FYVE fingers, and a C-terminal coiled coil region. The FYVE domain in both Vps27p and Vac1p harbors a zinc-binding site composed of seven Cysteines and one Histidine, which is different from that of other FYVE domain containing proteins.


Pssm-ID: 277275 [Multi-domain]  Cd Length: 56  Bit Score: 50.64  E-value: 6.48e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 157738667 1179 CLDCKREFSWMVRRHHCRICGRIFC-YYCCNNYVLSKHG-----GKKERCCRACF 1227
Cdd:cd15736     2 CHTCSRTFNLNIRAHHCRKCGKLFCrRHLPNMIPLNLSAydprnGKWYRCCHSCF 56
PTZ00121 PTZ00121
MAEBL; Provisional
 373-1108 6.48e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 57.84  E-value: 6.48e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  373 AMAQQKAD-TASDTKGRQEPIPSDAAQEMQELGEKLQALER--ERTKVEEVNRQQSAQLEQLVKELQlkEDARASLERLV 449
Cdd:PTZ00121 1083 AKEDNRADeATEEAFGKAEEAKKTETGKAEEARKAEEAKKKaeDARKAEEARKAEDARKAEEARKAE--DAKRVEIARKA 1160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  450 KEMAplQEELSGKGQEAdqlwRRLQEllAHTSSWEEELAELRREKKQQQEEKELLEQEVRSLTRQLQFLETQLAQVSQHV 529
Cdd:PTZ00121 1161 EDAR--KAEEARKAEDA----KKAEA--ARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKA 1232

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  530 SDL---EEQKKQLIQDKDHLSQQVGMLERLAGPPGPELPVAGE---KNEALVPVNSSLQEAWGKPEEEQRGLQEAQlddT 603
Cdd:PTZ00121 1233 EEAkkdAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEearKADELKKAEEKKKADEAKKAEEKKKADEAK---K 1309

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  604 KVQEGSQEEELRQANRELEKELQNVVGRNQLLEGKLQALQADYQALQQRESAIQGSLASLEAEQASIRHLGDQMEASLLA 683
Cdd:PTZ00121 1310 KAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEE 1389

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  684 VRKAKEAMK--------AQMAEKEAILQSKEGECQQLREEVEQCQQLAEARHRELRALESQCQQQtqliEVLTAEKGQQG 755
Cdd:PTZ00121 1390 KKKADEAKKkaeedkkkADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAE----EAKKAEEAKKK 1465

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  756 VGPPTDNEARELAAQLALSQAQLEvHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAVLREHKTLVQQLK---E 832
Cdd:PTZ00121 1466 AEEAKKADEAKKKAEEAKKADEAK-KKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKkaeE 1544

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  833 QNEALNRAHVQELLQCSEREGALQEERADE---------------AQQREEELRALQEELSQAKCSSEEAQLEHAELQEQ 897
Cdd:PTZ00121 1545 KKKADELKKAEELKKAEEKKKAEEAKKAEEdknmalrkaeeakkaEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEE 1624

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  898 LHRANTDTAELGIQVCALTVEKERVEEAL----ACAVQELQDAKEAASREREGLERQVAglQQEKESLQEKLKAAKAAAG 973
Cdd:PTZ00121 1625 LKKAEEEKKKVEQLKKKEAEEKKKAEELKkaeeENKIKAAEEAKKAEEDKKKAEEAKKA--EEDEKKAAEALKKEAEEAK 1702

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  974 SLPGLQAQLAQAEQRAQSLQEAahQELNTLKfqlsaeimdyqsrlknaGEECKslRGQLEEQGRQLQAAEEAVEKLKATQ 1053
Cdd:PTZ00121 1703 KAEELKKKEAEEKKKAEELKKA--EEENKIK-----------------AEEAK--KEAEEDKKKAEEAKKDEEEKKKIAH 1761

                         730       740       750       760       770
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 157738667 1054 ADMGEKLSCTSNHLAECQAAMLRKDKEGAALREDLERTQKELEKATTKIQEYYNK 1108
Cdd:PTZ00121 1762 LKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKE 1816
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 513-889 1.19e-07

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: 56.88  E-value: 1.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  513 RQLQFLETQLAQVSQHVSDLEEQKKQLIQD----KDHLS------QQVGMLERLAGPPGPELPVAGEKNEALVPVNSSLQ 582
Cdd:COG3096   299 RQLAEEQYRLVEMARELEELSARESDLEQDyqaaSDHLNlvqtalRQQEKIERYQEDLEELTERLEEQEEVVEEAAEQLA 378

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  583 EAwgkpeEEQRGLQEAQLDDTKVQEGSQEEEL----------RQANRELEKElQNVVGRNQL----LEGKLQALQADYQA 648
Cdd:COG3096   379 EA-----EARLEAAEEEVDSLKSQLADYQQALdvqqtraiqyQQAVQALEKA-RALCGLPDLtpenAEDYLAAFRAKEQQ 452

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  649 LQQRESAIQGSLASLEAEQAsirhlgdQMEASLLAVRKAKEAMKAQMAEKEAIlqskegecQQLREEVEQCQQLA----- 723
Cdd:COG3096   453 ATEEVLELEQKLSVADAARR-------QFEKAYELVCKIAGEVERSQAWQTAR--------ELLRRYRSQQALAQrlqql 517

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  724 EARHRELRALESQCQQQTQLIEVLTAEKGQQgvgpptdneaRELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAAL 803
Cdd:COG3096   518 RAQLAELEQRLRQQQNAERLLEEFCQRIGQQ----------LDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQL 587

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  804 DDQDKVQSQLSMAEAVLREHKTLVQQLKEQ-NEAL-NRAHVQELLQCS-EREGALQEERaDEAQQREEELRALQEELSQA 880
Cdd:COG3096   588 EQLRARIKELAARAPAWLAAQDALERLREQsGEALaDSQEVTAAMQQLlEREREATVER-DELAARKQALESQIERLSQP 666


                  ....*....
gi 157738667  881 KcSSEEAQL 889
Cdd:COG3096   667 G-GAEDPRL 674
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
606-832 1.22e-07

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 56.56  E-value: 1.22e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  606 QEGSQEEELRQANRELEKELQNVVGRNQLLEGKLQALQADYQ--ALQQRESAIQGSLASLEAEQASIRHLGDQMEASLLA 683
Cdd:COG3206   165 NLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGlvDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAA 244

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  684 VRKAKEAMKAQMAE--KEAILQSKEGECQQLREEVEQCQQLAEARHRELRALESQCQQQTQLIEvltaekgqqgvgpptd 761
Cdd:COG3206   245 LRAQLGSGPDALPEllQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQ---------------- 308

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157738667  762 neaRELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAVLREHKTLVQQLKE 832
Cdd:COG3206   309 ---QEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEE 376
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 860-1099 1.53e-07

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: 55.54  E-value: 1.53e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  860 ADEAQQREEELRALQEELSQAKCSSEEAQLEHAELQEQLHRANTDTAelgiqvcaltvekerveeALACAVQELQDAKEA 939
Cdd:COG4942    19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIA------------------ALARRIRALEQELAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  940 ASREREGLERQVAGLQQEKESLQEKLKA---AKAAAGSLPGLQAQLAQAEQRAQSLQEAAHQELNTLKFQLSAEIMDYQS 1016
Cdd:COG4942    81 LEAELAELEKEIAELRAELEAQKEELAEllrALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667 1017 RLKNAGEECKSLRGQLEEQGRQLQAAEEAVEKLKATQADMGEKLSCTSNHLAECQAAMLRKDKEGAALREDLERTQKELE 1096
Cdd:COG4942   161 ELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240


                  ...
gi 157738667 1097 KAT 1099
Cdd:COG4942   241 ERT 243
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 436-690 1.83e-07

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: 55.16  E-value: 1.83e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  436 QLKEDARASLERLVKEMAPLQEELSGKGQEADQLWRRLQELlahtssweeelaelrrekkqqqeekellEQEVRSLTRQL 515
Cdd:COG4942    20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAAL----------------------------ERRIAALARRI 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  516 QFLETQLAQVSQHVSDLEEQ----KKQLIQDKDHLSQQVGMLERLAGPPGPELPVAGEKNEALVPVNSSLQEAwgkpeEE 591
Cdd:COG4942    72 RALEQELAALEAELAELEKEiaelRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYL-----AP 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  592 QRGLQEAQLDDTKVQEGSQEEELRQANRELEKELQNVVGRNQLLEGKLQALQADYQALQQRESAIQGSLASLEAEQASIR 671
Cdd:COG4942   147 ARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELE 226

                         250
                  ....*....|....*....
gi 157738667  672 HLGDQMEASLLAVRKAKEA 690
Cdd:COG4942   227 ALIARLEAEAAAAAERTPA 245
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
316-963 1.83e-07

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 55.82  E-value: 1.83e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  316 QTCLQGLELGAAEKEE-DYHTALRRLEsmlqplaQELEATRDSLDKKNqhlasfpgwlamaqQKADTASDTKGRQEPIPS 394
Cdd:PRK02224  186 RGSLDQLKAQIEEKEEkDLHERLNGLE-------SELAELDEEIERYE--------------EQREQARETRDEADEVLE 244

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  395 DAAQEMQELGEKLQALERERTKVEEVNRQQSAQLEQLvkelqlkEDARASLERLVKEMAPLQEELSGKGQEADQLWRRLQ 474
Cdd:PRK02224  245 EHEERREELETLEAEIEDLRETIAETEREREELAEEV-------RDLRERLEELEEERDDLLAEAGLDDADAEAVEARRE 317

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  475 EllahtssweeelaelrrekkqqqeekelleqevrsLTRQLQFLETQLAQVSQHVSDLEEQKKQLIQDKDHLSQQvgmle 554
Cdd:PRK02224  318 E-----------------------------------LEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEER----- 357

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  555 rlagppgpelpvAGEKnealvpvnsslqeawgkpeEEQRGLQEAQLDDTKVQEGSQEEELrqanRELEKELQNVVGRNQL 634
Cdd:PRK02224  358 ------------AEEL-------------------REEAAELESELEEAREAVEDRREEI----EELEEEIEELRERFGD 402

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  635 LEGKLQALQADYQALQQRESAIQGSLASLEAEQASIRHlgdqmeasllAVRKAKEAMKAqmaekeailqSKEGECQQLRE 714
Cdd:PRK02224  403 APVDLGNAEDFLEELREERDELREREAELEATLRTARE----------RVEEAEALLEA----------GKCPECGQPVE 462

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  715 EVEQCQQLAEARHR------ELRALESQCQQQTQLIEVLTAEKGQQGVGPPTDNEARELAAQLALSQAQLEVHQGEVQRL 788
Cdd:PRK02224  463 GSPHVETIEEDRERveeleaELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEEL 542

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  789 QAQVVDLQAKMRAALDDQDKVQSQlsmAEAVLREHKTLVQQLKEQNEALNR-AHVQELL----QCSEREGALQEERADEA 863
Cdd:PRK02224  543 RERAAELEAEAEEKREAAAEAEEE---AEEAREEVAELNSKLAELKERIESlERIRTLLaaiaDAEDEIERLREKREALA 619

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  864 Q---QREEELRALQEELSQAKCSSEEAQLEhaELQEQLHRANTDTAELGIQVCALTVEKERVEEALACAVQELQDAKEAA 940
Cdd:PRK02224  620 ElndERRERLAEKRERKRELEAEFDEARIE--EAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEELR 697

                         650       660
                  ....*....|....*....|....*.
gi 157738667  941 SReREGLERQVAGLQ---QEKESLQE 963
Cdd:PRK02224  698 ER-REALENRVEALEalyDEAEELES 722
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 590-802 2.33e-07

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: 54.77  E-value: 2.33e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  590 EEQRGLQEAQLDDTKVQEGSQEEELRQANREL---EKELQNVVGRNQLLEGKLQALQADYQALQQRESAIQGSLASLEAE 666
Cdd:COG4942    33 QQEIAELEKELAALKKEEKALLKQLAALERRIaalARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRA 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  667 QASIRHLG-----------DQMEASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEVEQCQQLAEARHRELRALES 735
Cdd:COG4942   113 LYRLGRQPplalllspedfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEA 192

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157738667  736 QCQQQTQLIevltaekgqqgvgpptdneaRELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAA 802
Cdd:COG4942   193 LKAERQKLL--------------------ARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
849-1167 2.40e-07

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 55.43  E-value: 2.40e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  849 SEREGALQEERADEAQQREEELRALQEELSQaKCSSEEAQLEHAELQEQLHRANTDTAELgiqvcALTVEKERVEE--AL 926
Cdd:PRK02224  183 SDQRGSLDQLKAQIEEKEEKDLHERLNGLES-ELAELDEEIERYEEQREQARETRDEADE-----VLEEHEERREEleTL 256

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  927 ACAVQELQDAKEAASREREGLERQVAGLQQEKESLQEKLKAAKAAAG----SLPGLQAQLAQAEQRAQSLQE------AA 996
Cdd:PRK02224  257 EAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGlddaDAEAVEARREELEDRDEELRDrleecrVA 336

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  997 HQELNTLKFQLSAEIMDYQSRLKNAGEECKSL-------RGQLEEQGRQLQAAEEAVEKLKATQADMGEKLSCTSNHLAE 1069
Cdd:PRK02224  337 AQAHNEEAESLREDADDLEERAEELREEAAELeseleeaREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEE 416

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667 1070 CQAAMLRKDKEGAALREDLERTQKELEKATTKIQEYYNKLC-QEVTNRERNDQkmladLDDLNRTKKYLEERLIELLRDK 1148
Cdd:PRK02224  417 LREERDELREREAELEATLRTARERVEEAEALLEAGKCPECgQPVEGSPHVET-----IEEDRERVEELEAELEDLEEEV 491

                         330
                  ....*....|....*....
gi 157738667 1149 DALWQKSDALEFQQKLSAE 1167
Cdd:PRK02224  492 EEVEERLERAEDLVEAEDR 510
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 251-1143 2.41e-07

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: 55.82  E-value: 2.41e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   251 ERMQQLdreNQELRAAVSQQGEQLQTERERGRTAAEDNVRLTCLVAELQKQWEVTQATQNTVKELQTCLQGLE--LGAAE 328
Cdd:TIGR00606  189 ETLRQV---RQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEhnLSKIM 265

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   329 KEEDYHTALRRLESMLQPLAQELEATRDSL----DKKNQHLASFPGwlAMAQQKADTASDTKGRQEPIpsdaAQEMQELG 404
Cdd:TIGR00606  266 KLDNEIKALKSRKKQMEKDNSELELKMEKVfqgtDEQLNDLYHNHQ--RTVREKERELVDCQRELEKL----NKERRLLN 339

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   405 EKLQALERERTKVE---EVNRQQSAQLEQLVKELQLKEDAR-----ASLERLVKEMAPL-QEELSGKGQEADQLWRRLQE 475
Cdd:TIGR00606  340 QEKTELLVEQGRLQlqaDRHQEHIRARDSLIQSLATRLELDgfergPFSERQIKNFHTLvIERQEDEAKTAAQLCADLQS 419

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   476 LLAHTsswEEELAELRREKKQQQEEKELLEQEVRSLTRQLQFLETQLAQVSQHVSDLEEQKKQLIQDKDHLSqqvgMLER 555
Cdd:TIGR00606  420 KERLK---QEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELS----KAEK 492

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   556 LAGPPGPELPVAGEKNEALVPVNSSLQEAWGKPEEEQRGLQEAQLDDTKVQEGSQEEELRQANRELEKELQNVVG---RN 632
Cdd:TIGR00606  493 NSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGyfpNK 572

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   633 QLLEGKLQALQADYQALQQRESAIQGSLASLEAEQASIRHLGDQMEASLLAVR-KAKEAMKAQmaekeailqSKEGECQQ 711
Cdd:TIGR00606  573 KQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEdKLFDVCGSQ---------DEESDLER 643

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   712 LREEVEQCQQ----LAEARH------RELRALESQC--------QQQTQLIEVLTAEKGQQGVGP----PTDNEARELAA 769
Cdd:TIGR00606  644 LKEEIEKSSKqramLAGATAvysqfiTQLTDENQSCcpvcqrvfQTEAELQEFISDLQSKLRLAPdklkSTESELKKKEK 723

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   770 QLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEA-------------VLREHKTLVQQLKEQNEA 836
Cdd:TIGR00606  724 RRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETllgtimpeeesakVCLTDVTIMERFQMELKD 803

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   837 LNRAHVQEL--LQCSEREGALQEERaDEAQQREEELRALQEELSQAKCSSEEAQLEHAELQEQLHRANTDTAELGIQVCA 914
Cdd:TIGR00606  804 VERKIAQQAakLQGSDLDRTVQQVN-QEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQR 882

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   915 LTVEKERVEEaLACAVQELQDAKEAASREREGLERQVAGLQQEKESLQeklkaakaaagslpglqaqlaqaeQRAQSLQE 994
Cdd:TIGR00606  883 RQQFEEQLVE-LSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELI------------------------SSKETSNK 937

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   995 AAHQELNTLKFQLSAEIMDYQSRLKNAGEECKSLRGQLEEQGRQLQAA-EEAVEKLKATQADMGE-KLSCTSNHLAEC-- 1070
Cdd:TIGR00606  938 KAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQKETELNTVNAQlEECEKHQEKINEDMRLmRQDIDTQKIQERwl 1017

                          890       900       910       920       930       940       950
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157738667  1071 --QAAMLRKDKEGAALREDLERTQKEL-EKATTKIQEYYNKLCQEVTNRERNDQKMLADLDDLNRTKKYLEERLIE 1143
Cdd:TIGR00606 1018 qdNLTLRKRENELKEVEEELKQHLKEMgQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELRE 1093
FYVE_MTMR_unchar cd15738
FYVE-related domain found in uncharacterized myotubularin-related proteins mainly from ...
 1170-1227 2.47e-07

FYVE-related domain found in uncharacterized myotubularin-related proteins mainly from eumetazoa; This family includes a group of uncharacterized myotubularin-related proteins mainly found in eumetazoa. Although their biological functions remain unclear, they share similar domain architecture that consists of an N-terminal pleckstrin homology (PH) domain, a highly conserved region related to myotubularin proteins, a C-terminal FYVE domain. The model corresponds to the FYVE domain, which resembles the FYVE-related domain as it has an altered sequence in the basic ligand binding patch.


Pssm-ID: 277277 [Multi-domain]  Cd Length: 61  Bit Score: 48.86  E-value: 2.47e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667 1170 WLGDTEANHClDCKREFSWMVRRHHCRICGRIFCYYCCNNYV-LSKH-GGKKERCCRACF 1227
Cdd:cd15738     3 WKSFRNVTEC-SCSTPFDHFSKKHHCWRCGNVFCTRCIDKQRaLPGHlSQRPVPVCRACY 61
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 241-597 2.69e-07

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: 55.46  E-value: 2.69e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   241 QLEVREKQLRERMQQLDRENQELRAAVSQQgEQLQTERERGRTAAEDNVRltclvaELQKQWEVTQATQNTVKELQTclq 320
Cdd:TIGR02169  671 SEPAELQRLRERLEGLKRELSSLQSELRRI-ENRLDELSQELSDASRKIG------EIEKEIEQLEQEEEKLKERLE--- 740

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   321 glelgaaekeedyhtalrRLESMLQPLAQELEATRDSLDKKNQHLasfpgwlamAQQKADTASDTKGRQEPIPSDAAQEM 400
Cdd:TIGR02169  741 ------------------ELEEDLSSLEQEIENVKSELKELEARI---------EELEEDLHKLEEALNDLEARLSHSRI 793

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   401 QELGEKLQALERERTKVEEVNRQQSAQLEQLVKELQLKEDARASLERLVKEmapLQEELSGKGQEADQLWRRLQELLAHT 480
Cdd:TIGR02169  794 PEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRID---LKEQIKSIEKEIENLNGKKEELEEEL 870

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   481 SSWEEELAELRREKKQQQEEKELLEQEVRSLTRQLQFLETQLAQVSQHVSDLEEQKKQLIQDKDHLSQQVGMLErlagPP 560
Cdd:TIGR02169  871 EELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDE----EI 946

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157738667   561 GPELPVAG----------EKNEALVPVN--------------SSLQEAWGKPEEEQRGLQE 597
Cdd:TIGR02169  947 PEEELSLEdvqaelqrveEEIRALEPVNmlaiqeyeevlkrlDELKEKRAKLEEERKAILE 1007
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 939-1177 2.90e-07

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: 54.38  E-value: 2.90e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  939 AASREREGLERQVAGLQQEKESLQEKLKAAKAAAGSlpgLQAQLAQAEQRAQSLQEAAhQELNTLKFQLSAEIMDYQSRL 1018
Cdd:COG4942    17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKA---LLKQLAALERRIAALARRI-RALEQELAALEAELAELEKEI 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667 1019 KNAGEECKSLRGQLEEQGRQLQAAEEAVE-KLKATQAD------MGEKLSCTSNHLAECQAAMLRKDKEGAALREDLERT 1091
Cdd:COG4942    93 AELRAELEAQKEELAELLRALYRLGRQPPlALLLSPEDfldavrRLQYLKYLAPARREQAEELRADLAELAALRAELEAE 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667 1092 QKELEKATTKIQEYYNKLCQEVTNRERNdqkmladLDDLNRTKKYLEERLIELLRDKDALWQKSDALEFQQKLSAEERWL 1171
Cdd:COG4942   173 RAELEALLAELEEERAALEALKAERQKL-------LARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245


                  ....*.
gi 157738667 1172 GDTEAN 1177
Cdd:COG4942   246 AGFAAL 251
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
784-1166 3.18e-07

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 55.16  E-value: 3.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  784 EVQRLQAQVVDLQAKM---RAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNEAlnRAHVQELLQCsEREGALQEERA 860
Cdd:COG4717    72 ELKELEEELKEAEEKEeeyAELQEELEELEEELEELEAELEELREELEKLEKLLQL--LPLYQELEAL-EAELAELPERL 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  861 DEAQQREEELRALQEELsqakcssEEAQLEHAELQEQLHRANTDTAELGIQvcALTVEKERVEEALAcAVQELQDAKEAA 940
Cdd:COG4717   149 EELEERLEELRELEEEL-------EELEAELAELQEELEELLEQLSLATEE--ELQDLAEELEELQQ-RLAELEEELEEA 218

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  941 SREREGLERQVAGLQQEKESLQEK------------------LKAAKAAAGSLP-----------GLQAQLAQAEQRAQS 991
Cdd:COG4717   219 QEELEELEEELEQLENELEAAALEerlkearlllliaaallaLLGLGGSLLSLIltiagvlflvlGLLALLFLLLAREKA 298

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  992 LQEAAHQELNTLKFQLSAEIMDYQSRLKNAGEECKSLRGQLEEQGRQLQAAEEAVEKLKATQADMGEKLSCTSNH--LAE 1069
Cdd:COG4717   299 SLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAalLAE 378

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667 1070 CQAAMLRKDKEGAALREDLERTQKELEKATTKIQEYYNKLCQEVtnRERNDQKMLADLDDLNRTKKYLEERLIELLRDKD 1149
Cdd:COG4717   379 AGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELL--EALDEEELEEELEELEEELEELEEELEELREELA 456

                         410
                  ....*....|....*..
gi 157738667 1150 ALWQKSDALEFQQKLSA 1166
Cdd:COG4717   457 ELEAELEQLEEDGELAE 473
RUN_RUFY1 cd17694
RUN domain found in RUN and FYVE domain-containing protein 1 (RUFY1) and similar proteins; ...
 32-135 5.35e-07

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: 51.06  E-value: 5.35e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   32 GEPITDDSTSLHKFSYKLEYLLQFDQKEKATLLGNKKDYWDYFCACLAKVKGANDGIRFVKSISELRTSLGKGRAFIRYS 111
Cdd:cd17694    24 GRTLDSDYPPLQQFFVVLEHCLKHGLKVKKSFIGQNKSFFGPLELVEKLCPEASDIATSARNLPELKTAVGRGRAWLHLA 103

                          90       100
                  ....*....|....*....|....
gi 157738667  112 LVHQRLADTLQQCFMNTKVTSDWY 135
Cdd:cd17694   104 LMQKKLADYLKVLIDRKDLLSEFY 127
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 690-941 7.15e-07

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: 53.23  E-value: 7.15e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  690 AMKAQMAEKEAILQSKEGECQQLREEVEQCQQLAEARHRELRALESQCQQQTQLIEVLTAEKGQqgvgppTDNEARELAA 769
Cdd:COG4942    17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAA------LEAELAELEK 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  770 QLALSQAQLEVHQGEVQRL--QAQVVDLQAKMRAALDDQDKVQSQ--LSMAEAVLREHKTLVQQLKEQNEALNRAHvqel 845
Cdd:COG4942    91 EIAELRAELEAQKEELAELlrALYRLGRQPPLALLLSPEDFLDAVrrLQYLKYLAPARREQAEELRADLAELAALR---- 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  846 lqcseregALQEERADEAQQREEELRALQEELSQAKcsseeaqlehAELQEQLHRANTDTAELGIQVCALTVEKERVEEA 925
Cdd:COG4942   167 --------AELEAERAELEALLAELEEERAALEALK----------AERQKLLARLEKELAELAAELAELQQEAEELEAL 228

                         250
                  ....*....|....*.
gi 157738667  926 LACAVQELQDAKEAAS 941
Cdd:COG4942   229 IARLEAEAAAAAERTP 244
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 638-887 8.08e-07

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: 53.23  E-value: 8.08e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  638 KLQALQADYQALQQRESAIQGSLASLEAEQASIRHLGDQMEASLLAVRKAKEAMKAQMAEKEAILQskegecqQLREEVE 717
Cdd:COG4942    21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELA-------ELEKEIA 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  718 QCQQLAEARHRELRALESQCQ---QQTQLIEVLTAEkgqqgvgpptdnEARELAAQLALSQAQLEVHQGEVQRLQAQVVD 794
Cdd:COG4942    94 ELRAELEAQKEELAELLRALYrlgRQPPLALLLSPE------------DFLDAVRRLQYLKYLAPARREQAEELRADLAE 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  795 LQAKMRAALDDQDKVQSQLSMAEAvlrEHKTLVQQLKEQNEALNRAhvqellqcsEREGALQEERADEAQQREEELRALQ 874
Cdd:COG4942   162 LAALRAELEAERAELEALLAELEE---ERAALEALKAERQKLLARL---------EKELAELAAELAELQQEAEELEALI 229

                         250
                  ....*....|...
gi 157738667  875 EELSQAKCSSEEA 887
Cdd:COG4942   230 ARLEAEAAAAAER 242
RUN_RUNDC3B cd17700
RUN domain found in RUN domain-containing protein 3B (RUNDC3B) and similar proteins; RUN ...
 33-135 8.16e-07

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: 50.35  E-value: 8.16e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   33 EPITDDSTSLHKFSYKLEYLLQFDQKEKATLLG--NKKDYWDYFCACLAKVkgANDGIRFVKSISELRTSLGKGRAFIRY 110
Cdd:cd17700    20 ETIDDSSPEFVNFAAILEQILSHRLKGQVTWFGyeSPRSFWDYIRVACSKV--PHNCICSIENMENVSSSRAKGRAWIRV 97

                          90       100
                  ....*....|....*....|....*
gi 157738667  111 SLVHQRLADTLQQCFMNTKVTSDWY 135
Cdd:cd17700    98 ALMEKRLSEYISTALRDFKTTRRFY 122
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 515-871 8.55e-07

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: 53.80  E-value: 8.55e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  515 LQFLETQLAQVSQHVSDLEEQKKQLIQDKDHLSQQVGMLERLagppgpeLPVAGEKNEAlvpvnsSLQEAWGKPEEEQRG 594
Cdd:COG3096   838 LAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKL-------LPQANLLADE------TLADRLEELREELDA 904

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  595 LQEAQLddtkvqegsqeeELRQANRELEkELQNVVGRNQLLEGKLQALQADYQALQQRESAIQGSLASLEAEQASIRHLG 674
Cdd:COG3096   905 AQEAQA------------FIQQHGKALA-QLEPLVAVLQSDPEQFEQLQADYLQAKEQQRRLKQQIFALSEVVQRRPHFS 971

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  675 DQMEASLLAVRKA-KEAMKAQMAEKEAilqskegECQQLREEVEQCQQLAEARHRELRALESQCQQQTQLIEVLTAEKGQ 753
Cdd:COG3096   972 YEDAVGLLGENSDlNEKLRARLEQAEE-------ARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEE 1044

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  754 QGVGPPTDNEAR------ELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAvlreHKTLV 827
Cdd:COG3096  1045 LGVQADAEAEERarirrdELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQVVQAKA----GWCAV 1120

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 157738667  828 QQLKEQNEALNRAHVQELLQCSERE---------GALQEERADeaqqrEEELR 871
Cdd:COG3096  1121 LRLARDNDVERRLHRRELAYLSADElrsmsdkalGALRLAVAD-----NEHLR 1168
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 611-965 8.90e-07

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 53.36  E-value: 8.90e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   611 EEELRQANRELEKELQNVVGRNQLLEGKLQALQADYQALQQRESAIQGSLASLEAEQASIRHLGDQMEASLLAVRKAKEA 690
Cdd:pfam07888   33 QNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEE 112

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   691 MKAqmaEKEAILQSKEGECQQLREEVEQCQQLAE---ARHRELRALESQCQQQT-QLIEVLTAEKGQQGVGPPTDNEARE 766
Cdd:pfam07888  113 LSE---EKDALLAQRAAHEARIRELEEDIKTLTQrvlERETELERMKERAKKAGaQRKEEEAERKQLQAKLQQTEEELRS 189

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   767 LAAQLALSQAQLEVHQGEVQRLQAQVVDLQ----------AKMRAALDDQDKVQSQLSM----AEAVLREHKTLVQQLKE 832
Cdd:pfam07888  190 LSKEFQELRNSLAQRDTQVLQLQDTITTLTqklttahrkeAENEALLEELRSLQERLNAserkVEGLGEELSSMAAQRDR 269

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   833 QNEALNRAHVQEL---LQCSEREGALQEERADEAQQREEELRALQEELSQAKCSSEEAQLEHAELQEQLHRANTDTAELG 909
Cdd:pfam07888  270 TQAELHQARLQAAqltLQLADASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVELG 349

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 157738667   910 IQV-CALTVEKERVEEalacaVQELQDAKEAASREREGLERQVAGLQQEKESLQEKL 965
Cdd:pfam07888  350 REKdCNRVQLSESRRE-----LQELKASLRVAQKEKEQLQAEKQELLEYIRQLEQRL 401
FYVE1_Vac1p_like cd15761
FYVE-related domain 1 found in yeast protein VAC1 (Vac1p) and similar proteins; Vac1p, also ...
 1170-1238 9.98e-07

FYVE-related domain 1 found in yeast protein VAC1 (Vac1p) and similar proteins; Vac1p, also termed vacuolar segregation protein Pep7p, or carboxypeptidase Y-deficient protein 7, or vacuolar protein sorting-associated protein 19 (Vps19p), or vacuolar protein-targeting protein 19, is a phosphatidylinositol 3-phosphate (PtdIns3P or PI3P)-binding protein that interacts with a Rab GTPase, GTP-bound form of Vps21p, and a Sec1p homologue, Vps45p, to facilitate Vps45p-dependent vesicle-mediated vacuolar protein sorting. It also acts as a novel regulator of vesicle docking and/or fusion at the endosome and functions in vesicle-mediated transport of Golgi precursor carboxypeptidase Y (CPY), protease A (PrA), protease B (PrB), but not alkaline phosphatase (ALP) from the trans-Golgi network-like compartment (TGN) to the endosome. Vac1p contains an N-terminal classical TFIIIA-like zinc finger, two putative zinc-binding FYVE fingers, and a C-terminal coiled coil region. The family corresponds to the first FYVE domain, which resembles the FYVE-related domain as it has an altered sequence in the basic ligand binding patch.


Pssm-ID: 277300  Cd Length: 76  Bit Score: 47.65  E-value: 9.98e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157738667 1170 WLGDTEANHCLDCKREFSWMVRRHHCRICGRIFCYYCCNNYV-LSKHG------GKKERCCRACFqklSEGPGSPD 1238
Cdd:cd15761     4 WKKPSGKSRCSECGKTLNKKNGIVNCRKCGELFCNEHCRNRIkLNNSAeydpknGKWCRCCEKCF---TSRPGYND 76
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
648-1169 1.03e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 53.53  E-value: 1.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  648 ALQQRESAIQGSLASLEAEQASIRH-LG-DQMEASLLAVRKAKEAMKAQMAEKEAILQSKEgECQQLREEVEQcqQLAEA 725
Cdd:PRK03918  129 AIYIRQGEIDAILESDESREKVVRQiLGlDDYENAYKNLGEVIKEIKRRIERLEKFIKRTE-NIEELIKEKEK--ELEEV 205

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  726 RhRELRALESQCQQQTQLIEVLTAEKgqqgvgpptdNEARELAAQLALSQAQLEVHQGEVQRLQAQVVDLQ---AKMRAA 802
Cdd:PRK03918  206 L-REINEISSELPELREELEKLEKEV----------KELEELKEEIEELEKELESLEGSKRKLEEKIRELEeriEELKKE 274

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  803 LDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNEALNRahVQELLQCSEREGALQEERADEAQQREEELRALQEELSQAKC 882
Cdd:PRK03918  275 IEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELRE--IEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEK 352

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  883 SSEEAQLEHAELQE---QLHRANTDTAELGIQvcaltvEKERVEEALacavQELQDAKEAASREREGLERQVAGLQQEKE 959
Cdd:PRK03918  353 RLEELEERHELYEEakaKKEELERLKKRLTGL------TPEKLEKEL----EELEKAKEEIEEEISKITARIGELKKEIK 422

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  960 SLQEKLKAAKAAAGSLPGLQAQLAqaEQRAQSLQEAAHQELNtlkfQLSAEIMDYQSRLKNAGEECKSLRGQLEEQgRQL 1039
Cdd:PRK03918  423 ELKKAIEELKKAKGKCPVCGRELT--EEHRKELLEEYTAELK----RIEKELKEIEEKERKLRKELRELEKVLKKE-SEL 495

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667 1040 QAAEEAVEKLKATQadmgEKLSCTSnhlaecqaamlrkdkegaalREDLERTQKELEKattkIQEYYNKLCQEVTNRERN 1119
Cdd:PRK03918  496 IKLKELAEQLKELE----EKLKKYN--------------------LEELEKKAEEYEK----LKEKLIKLKGEIKSLKKE 547

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|
gi 157738667 1120 dqkmLADLDDLNRTKKYLEERLIELLRDKDALWQKSDALEFQQKLSAEER 1169
Cdd:PRK03918  548 ----LEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEER 593
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 579-1111 1.04e-06

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 53.57  E-value: 1.04e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   579 SSLQEAWGKPEEEQRGLQEAQLDDTKV----QEGSQE--------------------------EELRQANRELEKELQNV 628
Cdd:pfam05483  106 NKLQENRKIIEAQRKAIQELQFENEKVslklEEEIQEnkdlikennatrhlcnllketcarsaEKTKKYEYEREETRQVY 185

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   629 VGRNQLLEGKLQALQadyQALQQRESAIQGSLASLEAEQASIRHLGDQMEASLLAVRKAKEAMKAQMAEKEA-------I 701
Cdd:pfam05483  186 MDLNNNIEKMILAFE---ELRVQAENARLEMHFKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENkmkdltfL 262

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   702 LQSKEGECQQLREEV----EQCQQLAEARHRELRALES-QCQQQTQLIEVLTAEKGQQGVGPPTDNEARELAAQLALSQA 776
Cdd:pfam05483  263 LEESRDKANQLEEKTklqdENLKELIEKKDHLTKELEDiKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNK 342

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   777 QLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAVLREHKTLVQQLKE--QNEALNRAHVQELLqcSEREGA 854
Cdd:pfam05483  343 AKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKfkNNKEVELEELKKIL--AEDEKL 420

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   855 LQEERADEA----------------QQREEELRALQEELSQAKCSSEEAQLEHAELQEQLHRANTDTAELGIQVCALTVE 918
Cdd:pfam05483  421 LDEKKQFEKiaeelkgkeqelifllQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLE 500

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   919 KERVEEALACAVQELQDAKE---AASREREGLERQVAGLQQEKESLQEKLKAAKAA-AGSLPGLQAQLAQAEQRAQSLQE 994
Cdd:pfam05483  501 NKELTQEASDMTLELKKHQEdiiNCKKQEERMLKQIENLEEKEMNLRDELESVREEfIQKGDEVKCKLDKSEENARSIEY 580

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   995 AAHQELNTLKF------QLSAEIMDYQSRLKNAGEECKSLRGQLEEQGRQLQAAEEAVEKLKATQADMGEKL-SCTSNHL 1067
Cdd:pfam05483  581 EVLKKEKQMKIlenkcnNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFeEIIDNYQ 660

                          570       580       590       600
                   ....*....|....*....|....*....|....*....|....
gi 157738667  1068 AECQAAMLRKDKegaaLREDLERTQKELEKAtTKIQEYYNKLCQ 1111
Cdd:pfam05483  661 KEIEDKKISEEK----LLEEVEKAKAIADEA-VKLQKEIDKRCQ 699
RUN_RUFY2 cd17695
RUN domain found in RUN and FYVE domain-containing protein 2 (RUFY2) and similar proteins; ...
 32-164 1.15e-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: 49.98  E-value: 1.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   32 GEPITDDSTSLHKFSYKLEYLLQFDQKEKATLLGNKKDYWDYFCACLAKVKGANDGIRFVKSISELRTSLGKGRAFIRYS 111
Cdd:cd17695    24 GRTLDSDYPPLQQFFVVMEHCLKHGLKVRKSFLSYNKTIWGPLELVEKLCPEAEEIAASVRDLPGLKTPLGRARAWLRLA 103

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 157738667  112 LVHQRLADTLQQCFMNTKVTSDWYYARSPFLQPKlSSDIVGQLYELTEVQFDL 164
Cdd:cd17695   104 LMQKKLADYLRCLIIRRDLLSEFYEYHALMMEEE-GAVIVGLLVGLNVIDANL 155
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 514-740 1.16e-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: 52.46  E-value: 1.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  514 QLQFLETQLAQVSQHVSDLEEQKKQLIQDKDHLSQQVGMLERlagppgpelpvagekneALVPVNSSLQEAwgkpeEEQR 593
Cdd:COG4942    21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALER-----------------RIAALARRIRAL-----EQEL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  594 GLQEAQLDDTKVQEGSQEEELRQANRELEKELQNV--VGRNQLLEG------------KLQALQADYQALQQRESAIQGS 659
Cdd:COG4942    79 AALEAELAELEKEIAELRAELEAQKEELAELLRALyrLGRQPPLALllspedfldavrRLQYLKYLAPARREQAEELRAD 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  660 LASLEAEQASIRHLGDQMEASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEVEQCQQLAEARHRELRALESQCQQ 739
Cdd:COG4942   159 LAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238


                  .
gi 157738667  740 Q 740
Cdd:COG4942   239 A 239
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 813-1159 1.21e-06

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 53.10  E-value: 1.21e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   813 LSMAEAVLREHKTLVQQ---LKEQNEALNRAhvqellqcseregalQEERADEAQQREEELRALQEELSQAKCSSEEAQL 889
Cdd:TIGR04523  203 LSNLKKKIQKNKSLESQiseLKKQNNQLKDN---------------IEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKK 267

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   890 EHAELQEQLHRANTDTAELGIQVCALTVE-----KERVEEALACAVQELQDAKEaasrEREGLERQVAGLQQEKESLQEK 964
Cdd:TIGR04523  268 QLSEKQKELEQNNKKIKELEKQLNQLKSEisdlnNQKEQDWNKELKSELKNQEK----KLEEIQNQISQNNKIISQLNEQ 343

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   965 LKAAKAAAGSLPG----LQAQLAQAEQRAQSLQEAAHQELNTLKfQLSAEIMDYQSRLKNAGEECKSLRGQLEEQGRQLQ 1040
Cdd:TIGR04523  344 ISQLKKELTNSESenseKQRELEEKQNEIEKLKKENQSYKQEIK-NLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKE 422

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  1041 AAEEAVEKLKATQADMGEKLSCTSNhlaecqaamlrKDKEGAALREDLERTQKELEKATTKIQEYYNKLCQEVTNRERND 1120
Cdd:TIGR04523  423 LLEKEIERLKETIIKNNSEIKDLTN-----------QDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKEL 491

                          330       340       350
                   ....*....|....*....|....*....|....*....
gi 157738667  1121 QKMLADLDDLNRTKKYLEERLIELLRDKDALWQKSDALE 1159
Cdd:TIGR04523  492 KSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLE 530
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 403-806 1.30e-06

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 52.98  E-value: 1.30e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   403 LGEKLQALERERTkveEVNRQQSAQLEQLVKELQLKEDARASLERLVKEM----APLQEELSGKGQEADQLWRRLQELLA 478
Cdd:pfam07888   32 LQNRLEECLQERA---ELLQAQEAANRQREKEKERYKRDREQWERQRRELesrvAELKEELRQSREKHEELEEKYKELSA 108

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   479 HTSSWEEELAELRREKKQQQEEKELLEQEVRSLTRQLQFLETQLAQVSQHVSDLEEQKKQLIQDKDHLSQQVGMLErlag 558
Cdd:pfam07888  109 SSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTE---- 184

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   559 ppgpelpvageknEALVPVNSSLQEAwgKPEEEQRGLQEAQLDDTKVQegsqeeelrqanrelekeLQNVVGRNQLLEGK 638
Cdd:pfam07888  185 -------------EELRSLSKEFQEL--RNSLAQRDTQVLQLQDTITT------------------LTQKLTTAHRKEAE 231

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   639 LQALQADYQALQQRESAIQGSLASLEAEQASIRHLGDQMEASLLAVRKAKEAMKAQMAekEAILQSKEGECQQLREEvEQ 718
Cdd:pfam07888  232 NEALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQARLQAAQLTLQLA--DASLALREGRARWAQER-ET 308

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   719 CQQLAEARH-------RELRALESQCQQQTQLIEVLTAEKGQQ-----GVGPPTDNEARELAAQLALSQAQLEVHQGEVQ 786
Cdd:pfam07888  309 LQQSAEADKdrieklsAELQRLEERLQEERMEREKLEVELGREkdcnrVQLSESRRELQELKASLRVAQKEKEQLQAEKQ 388

                          410       420
                   ....*....|....*....|
gi 157738667   787 RLQAQVVDLQAKMRAALDDQ 806
Cdd:pfam07888  389 ELLEYIRQLEQRLETVADAK 408
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 681-1161 1.56e-06

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 53.05  E-value: 1.56e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   681 LLAVRKAKEAMKAQMAEKEAILQSKEGecqqlREEVEQCQQLAEARHRELRALESQCQQQTQLIEVLTAEKGQQgvgppt 760
Cdd:TIGR00618  148 LLPQGEFAQFLKAKSKEKKELLMNLFP-----LDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDT------ 216

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   761 dneARELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKmraaLDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNEALNRA 840
Cdd:TIGR00618  217 ---YHERKQVLEKELKHLREALQQTQQSHAYLTQKREA----QEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRA 289

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   841 --------HVQELLQCSEREGALQEERADEAQQREEELRALQEELSQAKCSSEEAQLEHAELQEQLHRANTDTAELGIQv 912
Cdd:TIGR00618  290 rkaaplaaHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIR- 368

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   913 caltvEKERVEEALACAVQELQDAKEAASREREGLERQVAGLQQEKESLQEKLKAAKAAAGSLPGLQAQLaQAEQRAQSL 992
Cdd:TIGR00618  369 -----EISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQ-ELQQRYAEL 442

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   993 QEAAHQELNTLKFQLSAEIMDYQSRLKNAGEECKSLRGQLEEQGRQLQAAEEAVEKLKATQADMGEKLSCTSNHLAEC-- 1070
Cdd:TIGR00618  443 CAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIdn 522

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  1071 ----QAAMLRKDKEGAALREDLERTQKELEKATTKIQEYYNK---LCQEVTNRERNDQKMLADLDDLNRTKKYLEERLIE 1143
Cdd:TIGR00618  523 pgplTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQmqeIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEK 602

                          490
                   ....*....|....*...
gi 157738667  1144 LLRDKDALWQKSDALEFQ 1161
Cdd:TIGR00618  603 LSEAEDMLACEQHALLRK 620
FYVE_WDFY1_like cd15718
FYVE domain found in WD40 repeat and FYVE domain-containing protein WDFY1 and WDFY2, and ...
 1174-1227 1.78e-06

FYVE domain found in WD40 repeat and FYVE domain-containing protein WDFY1 and WDFY2, and similar proteins; This family includes WD40 repeat and FYVE domain-containing protein WDFY1 and WDFY2. WDFY1, also termed FYVE domain containing protein localized to endosomes-1 (FENS-1), or phosphoinositide-binding protein 1, or zinc finger FYVE domain-containing protein 17, is a novel single FYVE domain containing protein that binds phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) with high specificity over other phosphoinositides. WDFY1 to early endosomes requires an intact FYVE domain and is inhibited by wortmannin, a PI3-kinase inhibitor. WDFY2, also termed zinc finger FYVE domain-containing protein 22, or ProF (propeller-FYVE protein), is a phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) binding protein that is localized to a distinct subset of early endosomes close to the plasma membrane. It interacts preferentially with endogenous serine/threonine kinase Akt2, but not Akt1, and plays a specific role in modulating signaling through Akt downstream of the interaction of this kinase with the endosomal proteins APPL (adaptor protein containing PH domain, PTB domain, and leucine zipper motif). In addition to Akt, WDFY2 serves as a binding partner for protein kinase C, zeta (PRKCZ), and its substrate vesicle-associated membrane protein 2 (VAMP2), and is involved in vesicle cycling in various secretory pathways. Moreover, Silencing of WDFY2 by siRNA produces a strong inhibition of endocytosis. Both WDFY1 and WDFY2 contain a FYVE domain and multiple WD-40 repeats.


Pssm-ID: 277258 [Multi-domain]  Cd Length: 70  Bit Score: 46.93  E-value: 1.78e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157738667 1174 TEANHCLDCKREFSW----M-------VRRHHCRICGRIFCYYCCNNY-VLSKHGGKKE-RCCRACF 1227
Cdd:cd15718     4 AESDNCQKCSRPFFWnfkqMwekktlgVRQHHCRKCGKAVCDKCSSNRsTIPVMGFEFPvRVCNECY 70
RUN pfam02759
RUN domain; This domain is present in several proteins that are linked to the functions of ...
 49-164 3.50e-06

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: 48.04  E-value: 3.50e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667    49 LEYLLQ------FDQKEKATLLGNKKDYWDYFCACLAKVKGANDGIRFVKSISELRT---SLGKGRAFIRYSLVHQRLAD 119
Cdd:pfam02759    6 LEALLShglkrsSLLILRAAGLLPERSFWALLERVGKLVPPAEELLSSVQELEQIHTpysPDGRGRAWIRLALNEKLLDQ 85

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 157738667   120 TLQQCFMNTKVTSDWYYARSPFLQPKLSSDIVGQLYELTEVQFDL 164
Cdd:pfam02759   86 WLKLLLSNKELLSEYYEPWALLADPEFGEILLGLLVGLSALDFNL 130
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
226-679 3.75e-06

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 51.58  E-value: 3.75e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  226 NEALEGFDEMRLELDQLEVREKQLRERMQQLDRENQELRAAVSQQGEQLQTERERgRTAAEDNVRLTCLVAE--LQKQWE 303
Cdd:PRK02224  240 DEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEE-RDDLLAEAGLDDADAEavEARREE 318

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  304 VTQATQNTVKELQTCLQGLEL------GAAEKEEDYHTALRRLESMLQPLAQELEATRDSLDKKNQHLASFPGWLAMAQQ 377
Cdd:PRK02224  319 LEDRDEELRDRLEECRVAAQAhneeaeSLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRE 398

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  378 KADTASDTKGRQEPIPSDAAQEMQELGEKLQALERERTKVEEVNRQQSAQLE--------QLVKE---LQLKEDARASLE 446
Cdd:PRK02224  399 RFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEagkcpecgQPVEGsphVETIEEDRERVE 478

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  447 RLVKEMAPLQEELSGKGQEADQLwRRLQELLAHTSSWEEELAELRREKKQQQEEKELLEQEVRSLTRQLQFLETQLAQ-- 524
Cdd:PRK02224  479 ELEAELEDLEEEVEEVEERLERA-EDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEkr 557

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  525 ------------VSQHVSDLEEQKKQLIQDKDHLSQQVGMLERLAGpPGPELPVAGEKNEALVPVNSSLQEAWGKPEEEQ 592
Cdd:PRK02224  558 eaaaeaeeeaeeAREEVAELNSKLAELKERIESLERIRTLLAAIAD-AEDEIERLREKREALAELNDERRERLAEKRERK 636

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  593 RGLqEAQLDDTKVqegsqeEELRQANRELEKELQNVvgrnqllEGKLQALQADYQALQQRESAIQGSLASLEAEQASIRH 672
Cdd:PRK02224  637 REL-EAEFDEARI------EEAREDKERAEEYLEQV-------EEKLDELREERDDLQAEIGAVENELEELEELRERREA 702


                  ....*..
gi 157738667  673 LGDQMEA 679
Cdd:PRK02224  703 LENRVEA 709
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
236-733 3.80e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 51.69  E-value: 3.80e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  236 RLELDQLEVREKQLRERMQQLDrENQELRAAVSQQGEQLQTERERgRTAAEDNVRLTCLVAELQKQWEVTQATQNTVKEL 315
Cdd:COG4717    67 ELNLKELKELEEELKEAEEKEE-EYAELQEELEELEEELEELEAE-LEELREELEKLEKLLQLLPLYQELEALEAELAEL 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  316 QTCLQGLElgaaEKEEDYHTALRRLESmlqpLAQELEATRDSLDKKNQHLaSFPGWLAMaqqkadtasdtkgrqepipSD 395
Cdd:COG4717   145 PERLEELE----ERLEELRELEEELEE----LEAELAELQEELEELLEQL-SLATEEEL-------------------QD 196

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  396 AAQEMQELGEKLQALERERTKVEEVNRQQSAQLEQLVKELQLKEDARaslerlvkemaplqeelsgKGQEADQLWRRLQE 475
Cdd:COG4717   197 LAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEE-------------------RLKEARLLLLIAAA 257

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  476 LLAHTSSWEEELAELRREKKQQQEEKELLEQEVRSLTRQLQFLETQLAQVSQHVSDLEEQKKQLIQDKDHLsqqvgmler 555
Cdd:COG4717   258 LLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAAL--------- 328

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  556 lagppGPELPVAGEKNEALVPVNSSLQEAWGKPEEEQRGLQEAQLddtkvqEGSQEEELRQANRELEKELQNVVGRNQLL 635
Cdd:COG4717   329 -----GLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEEL------EQEIAALLAEAGVEDEEELRAALEQAEEY 397

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  636 EGKLQALQADYQALQQRESAIQGSLASLEAEQASIRHlgDQMEASLLAVRKAKEAMKAQMAEKEAILQ--SKEGECQQLR 713
Cdd:COG4717   398 QELKEELEELEEQLEELLGELEELLEALDEEELEEEL--EELEEELEELEEELEELREELAELEAELEqlEEDGELAELL 475

                         490       500
                  ....*....|....*....|
gi 157738667  714 EEVEQCQQLAEARHRELRAL 733
Cdd:COG4717   476 QELEELKAELRELAEEWAAL 495
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
763-895 4.24e-06

Multidrug resistance efflux pump EmrA [Defense mechanisms];


Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 50.43  E-value: 4.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  763 EARELAAQLALSQAQLEVHQGEVQRLQAQVvDLQAKMRAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNEALNRAHV 842
Cdd:COG1566    77 DPTDLQAALAQAEAQLAAAEAQLARLEAEL-GAEAEIAAAEAQLAAAQAQLDLAQRELERYQALYKKGAVSQQELDEARA 155

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 157738667  843 QELLQCSEREGALQEERADEAQQRE-EELRALQEELSQAkcsseEAQLEHAELQ 895
Cdd:COG1566   156 ALDAAQAQLEAAQAQLAQAQAGLREeEELAAAQAQVAQA-----EAALAQAELN 204
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 762-999 4.46e-06

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 50.60  E-value: 4.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  762 NEARELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAVLREH----------KTLVQQL- 830
Cdd:COG3883    30 AELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERaralyrsggsVSYLDVLl 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  831 --KEQNEALNRAHVQELLQcseregALQEERADEAQQREEELRALQEELSQAKcssEEAQLEHAELQEQLHRANTDTAEL 908
Cdd:COG3883   110 gsESFSDFLDRLSALSKIA------DADADLLEELKADKAELEAKKAELEAKL---AELEALKAELEAAKAELEAQQAEQ 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  909 GIQVCALTVEKERVEEALACAVQELQDAKEAASREREGLERQVAGLQQEKESLQEKLKAAKAAAGSLPGLQAQLAQAEQR 988
Cdd:COG3883   181 EALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAG 260

                         250
                  ....*....|.
gi 157738667  989 AQSLQEAAHQE 999
Cdd:COG3883   261 SAGAAGAAAGA 271
RUN_RUFY3 cd17696
RUN domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar proteins; ...
 32-143 4.47e-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: 48.07  E-value: 4.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   32 GEPITDDSTSLHKFSYKLEYLLQFDQKEKATLLGNKKDYWDYFCACLAKVKGANDGIRFVKSISELRTSLGKGRAFIRYS 111
Cdd:cd17696    24 GRTLDSDYAPLQQFFVVMEHCLKHGLKAKKTFLGQNKSFWGPLELVEKLVPEAAEITASVKDLPGLKTPVGRGRAWLRLA 103

                          90       100       110
                  ....*....|....*....|....*....|..
gi 157738667  112 LVHQRLADTLQQCFMNTKVTSDWYYARSPFLQ 143
Cdd:cd17696   104 LMQKKLSEYMKALINRKDLLSEFYEPNALMME 135
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
609-1159 4.55e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 51.60  E-value: 4.55e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  609 SQEEELRQANRELEKELQNVVGRNQLLEGKLQALQADYQALQ---QRESAIQGSLASLEAEQASIRHLGDQMEASLLAVR 685
Cdd:PRK03918  186 KRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEkevKELEELKEEIEELEKELESLEGSKRKLEEKIRELE 265

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  686 KAKEAMKAQMAEkeaiLQSKEGECQQLREEVEqcqqlaeaRHRELRALESQCQQQTQLIEVLTAEKGQQGvgpptdNEAR 765
Cdd:PRK03918  266 ERIEELKKEIEE----LEEKVKELKELKEKAE--------EYIKLSEFYEEYLDELREIEKRLSRLEEEI------NGIE 327

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  766 ELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAalddqdkvqsqLSMAEAVLREHKTLVQQLKEQN-EALNRahvqE 844
Cdd:PRK03918  328 ERIKELEEKEERLEELKKKLKELEKRLEELEERHEL-----------YEEAKAKKEELERLKKRLTGLTpEKLEK----E 392

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  845 LLQCSEREGALQEE------RADEAQQREEELRALQEELSQAK-----CSSEEAQLEHAELQE----QLHRANTDTAELG 909
Cdd:PRK03918  393 LEELEKAKEEIEEEiskitaRIGELKKEIKELKKAIEELKKAKgkcpvCGRELTEEHRKELLEeytaELKRIEKELKEIE 472

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  910 IQVCALTVEKERVEEALAcAVQELQDAKEAASREREgLERQVAGLQQEKesLQEKLKAAKAAAGSLPGLQAQLAQAEQRA 989
Cdd:PRK03918  473 EKERKLRKELRELEKVLK-KESELIKLKELAEQLKE-LEEKLKKYNLEE--LEKKAEEYEKLKEKLIKLKGEIKSLKKEL 548

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  990 QSLQEaahqelntlkfqLSAEIMDYQSRLKNAGEECKSLRGQLEEQGrqLQAAEEAVEKLKATQADMGEKLScTSNHLAE 1069
Cdd:PRK03918  549 EKLEE------------LKKKLAELEKKLDELEEELAELLKELEELG--FESVEELEERLKELEPFYNEYLE-LKDAEKE 613

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667 1070 CQAAMLRKDKEGAAL---REDLERTQKELEKATTKI--------QEYYNKLCQEVTNRERNDQKMLADLDDLNRTKKYLE 1138
Cdd:PRK03918  614 LEREEKELKKLEEELdkaFEELAETEKRLEELRKELeelekkysEEEYEELREEYLELSRELAGLRAELEELEKRREEIK 693

                         570       580
                  ....*....|....*....|.
gi 157738667 1139 ERLIELLRDKDALWQKSDALE 1159
Cdd:PRK03918  694 KTLEKLKEELEEREKAKKELE 714
PRK10246 PRK10246
exonuclease subunit SbcC; Provisional
 610-1100 6.70e-06

exonuclease subunit SbcC; Provisional


Pssm-ID: 182330 [Multi-domain]  Cd Length: 1047  Bit Score: 50.95  E-value: 6.70e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  610 QEEELRQANRELEKELQNVVGRNQLLEGKLQALQADYQALQQRESAiQGSLASLEAEQ--ASIRHLGD---QMEASLLAV 684
Cdd:PRK10246  231 EEKQLLTAQQQQQQSLNWLTRLDELQQEASRRQQALQQALAAEEKA-QPQLAALSLAQpaRQLRPHWEriqEQSAALAHT 309

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  685 RKAKEAMKAQMAEKEA----ILQSKEGECQQLREEVEQCQQ-LAEAR-----HREL---RALESQC----QQQTQLIEVL 747
Cdd:PRK10246  310 RQQIEEVNTRLQSTMAlrarIRHHAAKQSAELQAQQQSLNTwLAEHDrfrqwNNELagwRAQFSQQtsdrEQLRQWQQQL 389

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  748 TAEKGQQGVGPPT--DNEARELAAQLALSQAQLEVHQgEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAVLREHKt 825
Cdd:PRK10246  390 THAEQKLNALPAItlTLTADEVAAALAQHAEQRPLRQ-RLVALHGQIVPQQKRLAQLQVAIQNVTQEQTQRNAALNEMR- 467

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  826 lvQQLKEQNEALNRahVQELLQCSEREGALQEERA---------------------------DEAQQR----EEELRALQ 874
Cdd:PRK10246  468 --QRYKEKTQQLAD--VKTICEQEARIKDLEAQRAqlqagqpcplcgstshpaveayqalepGVNQSRldalEKEVKKLG 543

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  875 EELSQAKcsseeAQLEhaELQEQLHRANTDTAELGIQVCALTVEKERVEEALACAVQELQDAK----EAASRERE----- 945
Cdd:PRK10246  544 EEGAALR-----GQLD--ALTKQLQRDESEAQSLRQEEQALTQQWQAVCASLNITLQPQDDIQpwldAQEEHERQlrlls 616

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  946 ----------GLERQVAGLQQEKESLQEKLKAAKAAAG-SLPGLQAQ---LAQAEQRAQSLQeAAHQELNTLKFQLSA-- 1009
Cdd:PRK10246  617 qrhelqgqiaAHNQQIIQYQQQIEQRQQQLLTALAGYAlTLPQEDEEaswLATRQQEAQSWQ-QRQNELTALQNRIQQlt 695

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667 1010 ---------EIMDYQS------RLKNAGEECKSLRGQLEEQGRQlqaaeEAVEKLKATQADMGEKLSCTSNHLAECQA-- 1072
Cdd:PRK10246  696 plletlpqsDDLPHSEetvaldNWRQVHEQCLSLHSQLQTLQQQ-----DVLEAQRLQKAQAQFDTALQASVFDDQQAfl 770

                         570       580
                  ....*....|....*....|....*...
gi 157738667 1073 AMLRKDKEGAALREDLERTQKELEKATT 1100
Cdd:PRK10246  771 AALLDEETLTQLEQLKQNLENQRQQAQT 798
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 226-452 8.46e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 50.83  E-value: 8.46e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   226 NEALEGFDEMRLELDQLEVREKQLRERMQQLDRENQELRAAVSQQGEQLQTERERGRTAAEDNVRLTCLVAELQKQWEVT 305
Cdd:TIGR02168  771 EEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEEL 850

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   306 QAT-----------QNTVKELQTCLQGLELGAAEKEEDYHTALRRLESM---LQPLAQELEATRDSLDKKNQHLASFPGW 371
Cdd:TIGR02168  851 SEDieslaaeieelEELIEELESELEALLNERASLEEALALLRSELEELseeLRELESKRSELRRELEELREKLAQLELR 930

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   372 LAMAQQKADT--------ASDTKGRQEPIPSDAAQEMQELGEKLQALERERTKVEEVN-------RQQSAQLEQLVKELQ 436
Cdd:TIGR02168  931 LEGLEVRIDNlqerlseeYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNlaaieeyEELKERYDFLTAQKE 1010

                          250
                   ....*....|....*.
gi 157738667   437 LKEDARASLERLVKEM 452
Cdd:TIGR02168 1011 DLTEAKETLEEAIEEI 1026
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 686-1167 9.84e-06

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 50.11  E-value: 9.84e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   686 KAKEAMKAQMAEKEAILQSKEGECQQLREEVEQ----CQQLAEARHRELRALESQCQQQTQLIEVLTAEKGQQgvgpptd 761
Cdd:pfam05483   85 KEAEKIKKWKVSIEAELKQKENKLQENRKIIEAqrkaIQELQFENEKVSLKLEEEIQENKDLIKENNATRHLC------- 157

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   762 NEARELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQdKVQSQLSMAEA--VLREHKTLVQQLKE--QNEAL 837
Cdd:pfam05483  158 NLLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEEL-RVQAENARLEMhfKLKEDHEKIQHLEEeyKKEIN 236

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   838 NRAHVQELL--QCSEREGALQ------EERADEAQQREEELRALQEELSQA--KCSSEEAQLEHAELQEQLHRANTDTAE 907
Cdd:pfam05483  237 DKEKQVSLLliQITEKENKMKdltfllEESRDKANQLEEKTKLQDENLKELieKKDHLTKELEDIKMSLQRSMSTQKALE 316

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   908 LGIQV-----CALTVEKErveealaCAVQELQDAKEAASREREGLERQVAGLQQEKESLQEKLKAAKAAAGSLP-GLQAQ 981
Cdd:pfam05483  317 EDLQIatktiCQLTEEKE-------AQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITmELQKK 389

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   982 LAQAEQRAQsLQEAAHQELNTLKFQLSAE--IMDYQSRLKNAGEEcksLRGQLEEQGRQLQAAEEAVEKLKATQADMGEK 1059
Cdd:pfam05483  390 SSELEEMTK-FKNNKEVELEELKKILAEDekLLDEKKQFEKIAEE---LKGKEQELIFLLQAREKEIHDLEIQLTAIKTS 465

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  1060 LSCTSNHLAECQAAMLR---KDKEGAALREDLERTQKELEKATTKIQEYYNKLCQEVTNRERNDQKMLADLDDLNRTKKY 1136
Cdd:pfam05483  466 EEHYLKEVEDLKTELEKeklKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMN 545

                          490       500       510
                   ....*....|....*....|....*....|.
gi 157738667  1137 LEErliELLRDKDALWQKSDALEFQQKLSAE 1167
Cdd:pfam05483  546 LRD---ELESVREEFIQKGDEVKCKLDKSEE 573
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 698-963 1.14e-05

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 49.89  E-value: 1.14e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   698 KEAILQSKEGECQQLREEVEQCQQLA------------------EARHRELRA----LESQCQQQTQLIEVLTAE-KGQQ 754
Cdd:pfam07888   28 RAELLQNRLEECLQERAELLQAQEAAnrqrekekerykrdreqwERQRRELESrvaeLKEELRQSREKHEELEEKyKELS 107

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   755 GVGPPTDNEARELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQN 834
Cdd:pfam07888  108 ASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEEL 187

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   835 EALNRAHVQELLQCSEREGALQE---------ERADEAQQRE-------EELRALQEELSQAKCSSEEAQLEHAEL---- 894
Cdd:pfam07888  188 RSLSKEFQELRNSLAQRDTQVLQlqdtittltQKLTTAHRKEaeneallEELRSLQERLNASERKVEGLGEELSSMaaqr 267

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157738667   895 ---QEQLHRANTDTAELGIQVCALTVEkerVEEALACAVQELQDAKEAASREREGLERQVAGLQQEKESLQE 963
Cdd:pfam07888  268 drtQAELHQARLQAAQLTLQLADASLA---LREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQE 336
FYVE_protrudin cd15723
FYVE-related domain found in protrudin and similar proteins; Protrudin, also termed zinc ...
 1179-1230 1.33e-05

FYVE-related domain found in protrudin and similar proteins; Protrudin, also termed zinc finger FYVE domain-containing protein 27 (ZFY27 or ZFYVE27), is a FYVE domain-containing protein involved in transport of neuronal cargoes and implicated in the onset of hereditary spastic paraplegia (HSP). It is involved in neurite outgrowth through binding to spastin. Moreover, it functions as a key regulator of the Rab11-dependent membrane trafficking during neurite extension. It serves as an adaptor molecule that links its associated proteins, such as Rab11-GDP, VAP-A and -B, Surf4, and RTN3, to KIF5, a motor protein that mediates anterograde vesicular transport in neurons, and thus plays a key role in the maintenance of neuronal function. The FYVE domain of protrudin resembles a FYVE-related domain that is structurally similar to the canonical FYVE domains but lacks the three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif. In addition, unlike canonical FYVE domains that is located to early endosomes and specifically binds to phosphatidylinositol 3-phosphate (PtdIns3P or PI3P), the FYVE domain of protrudin is located to plasma membrane and preferentially binds phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2), phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4)P2), and phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3). In addition to FYVE-related domain, protrudin also contains a Rab11-binding domain (RBD11), two hydrophobic domains, HP-1 and HP-2, an FFAT motif, and a coiled-coil domain.


Pssm-ID: 277262 [Multi-domain]  Cd Length: 62  Bit Score: 44.03  E-value: 1.33e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157738667 1179 CLDCKREFS-WMVRRHHCRICGRIFCYYCCNNYVLSKHGG------KKE--RCCRACFQKL 1230
Cdd:cd15723     2 CTGCGASFSvLLKKRRSCNNCGNAFCSRCCSKKVPRSVMGatapaaQREtvFVCSGCNDKL 62
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 246-1048 1.34e-05

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: 49.79  E-value: 1.34e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   246 EKQLRERMQQLDRENQElRAAVSQQGEQLQTERERGRTAAEDNVRLTCLVAELQKQWEvtQATQNTVKELQTCLQGLELG 325
Cdd:pfam01576  270 EAQISELQEDLESERAA-RNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRSKRE--QEVTELKKALEEETRSHEAQ 346

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   326 AAEKEEDYHTALRRLESMLQPLA---QELEATRDSLDKKNQHLasfpgwlamaQQKADTASDTKGRQEPIPSDAAQEMQE 402
Cdd:pfam01576  347 LQEMRQKHTQALEELTEQLEQAKrnkANLEKAKQALESENAEL----------QAELRTLQQAKQDSEHKRKKLEGQLQE 416

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   403 LGEKLQALERERTKVEEVNRQQSAQLEQLVKELqlkEDARASLERLVKEMAPLQEELsgkgQEADQLwrrLQELLAHTSS 482
Cdd:pfam01576  417 LQARLSESERQRAELAEKLSKLQSELESVSSLL---NEAEGKNIKLSKDVSSLESQL----QDTQEL---LQEETRQKLN 486

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   483 WEEELAELRREKKQQQEEKELLEQEVRSLTRQLQFLETQLA-------QVSQHVSDLEEQKKQLIQDKDHLSQQvgMLER 555
Cdd:pfam01576  487 LSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSdmkkkleEDAGTLEALEEGKKRLQRELEALTQQ--LEEK 564

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   556 LAGPPGPELP---VAGEKNEALVPVNSSLQEAwGKPEEEQRGLQEAQLDDTKVQEGSQEEELRQANRELEKELqnvvgRN 632
Cdd:pfam01576  565 AAAYDKLEKTknrLQQELDDLLVDLDHQRQLV-SNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKET-----RA 638

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   633 QLLEGKLQALQADYQALQQRESAIQGSLASLEAEQASIRHLGDQMEASLLAVRKAKEAMKAQMAEKEAILQSKEGecQQL 712
Cdd:pfam01576  639 LSLARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATED--AKL 716

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   713 REEVeqcqqlaearhrELRALESQCQQQTQLIEVLTAEKGQQGVgpptdNEARELAAQLALSQAQLEVHQGEVQRLQAQV 792
Cdd:pfam01576  717 RLEV------------NMQALKAQFERDLQARDEQGEEKRRQLV-----KQVRELEAELEDERKQRAQAVAAKKKLELDL 779

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   793 VDLQAKMRAALDDQDKVQSQLSMAEAVLREHKtlvqqlKEQNEAlnRAHVQELLQCSeregalqEERADEAQQREEELRA 872
Cdd:pfam01576  780 KELEAQIDAANKGREEAVKQLKKLQAQMKDLQ------RELEEA--RASRDEILAQS-------KESEKKLKNLEAELLQ 844

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   873 LQEELSQAKCSSEEAQLEHAELQEQLHRANTDTAelgiqvcALTVEKERVEEALACAVQELQDAKEAAsrerEGLERQVA 952
Cdd:pfam01576  845 LQEDLAASERARRQAQQERDELADEIASGASGKS-------ALQDEKRRLEARIAQLEEELEEEQSNT----ELLNDRLR 913

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   953 GLQQEKESLQEKLKAAKAAAGSLPGLQAQLaqaEQRAQSLQEAAHQELNTLKFQLSAEIMDYQSRLKNAGEeckslrgQL 1032
Cdd:pfam01576  914 KSTLQVEQLTTELAAERSTSQKSESARQQL---ERQNKELKAKLQEMEGTVKSKFKSSIAALEAKIAQLEE-------QL 983

                          810
                   ....*....|....*.
gi 157738667  1033 EEQGRQLQAAEEAVEK 1048
Cdd:pfam01576  984 EQESRERQAANKLVRR 999
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 777-1141 1.57e-05

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 49.63  E-value: 1.57e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   777 QLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAVLREHKTL-------VQQLKEQNEALNRAHVQELLQCS 849
Cdd:TIGR04523  233 NIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKikelekqLNQLKSEISDLNNQKEQDWNKEL 312

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   850 EREGALQEERADEAQ----QREEELRALQEELSQAKCSSEEAQLEHAELQEQLHRANTDTAELGIQVCALTVEKERVEEA 925
Cdd:TIGR04523  313 KSELKNQEKKLEEIQnqisQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQ 392

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   926 LACAVQELQDAKEaasrEREGLERQVAGLQQEKESLQEKLKAakaaagslpgLQAQLAQAEQRAQSLQEAAHQ------E 999
Cdd:TIGR04523  393 INDLESKIQNQEK----LNQQKDEQIKKLQQEKELLEKEIER----------LKETIIKNNSEIKDLTNQDSVkeliikN 458

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  1000 LNTLKFQLSAEIMDYQSRLKNAGEECKSLRGQLEEQGRQLQAAEEAVEKLKATQADMGEKLSCTSNHLAECQAAMLRKDK 1079
Cdd:TIGR04523  459 LDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKES 538

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157738667  1080 EGAALREDLER-----TQKELEKATTKIQEYYNKLCQEVTNRERNDQKMLADLDDLNRTKKYLEERL 1141
Cdd:TIGR04523  539 KISDLEDELNKddfelKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEI 605
PRK10246 PRK10246
exonuclease subunit SbcC; Provisional
 396-1042 2.05e-05

exonuclease subunit SbcC; Provisional


Pssm-ID: 182330 [Multi-domain]  Cd Length: 1047  Bit Score: 49.41  E-value: 2.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  396 AAQEMQELGEKLQALERERTKVEEVNRQQSAQLEQLVKELQLKEDARASLERLVKEMAPLQE--------ELSGKGQEAD 467
Cdd:PRK10246  214 TPEQVQSLTASLQVLTDEEKQLLTAQQQQQQSLNWLTRLDELQQEASRRQQALQQALAAEEKaqpqlaalSLAQPARQLR 293

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  468 QLWRRLQEllaHTSSWEEELAELRREKKQQQEEKELLEQEVRSLTRQLQFLETQLAQVSQHVSDLEE------------- 534
Cdd:PRK10246  294 PHWERIQE---QSAALAHTRQQIEEVNTRLQSTMALRARIRHHAAKQSAELQAQQQSLNTWLAEHDRfrqwnnelagwra 370

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  535 QKKQLIQDKDHLSQQVGML-----ERLAGPPGPELPVAGEKNEALVPVNsslqeawgkpeeEQRGLQEaQLDDTKVQEGS 609
Cdd:PRK10246  371 QFSQQTSDREQLRQWQQQLthaeqKLNALPAITLTLTADEVAAALAQHA------------EQRPLRQ-RLVALHGQIVP 437

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  610 QEEELRQANRELEKELQNVVGRNQLLEGKLQALQ------ADYQALQQRESAIqgslASLEAEQA------------SIR 671
Cdd:PRK10246  438 QQKRLAQLQVAIQNVTQEQTQRNAALNEMRQRYKektqqlADVKTICEQEARI----KDLEAQRAqlqagqpcplcgSTS 513

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  672 HLG-DQMEASLLAV----RKAKEAMKAQMAEKEAILQskeGECQQLREEVEQCQQLAEARHRELRALESQCQQqtqLIEV 746
Cdd:PRK10246  514 HPAvEAYQALEPGVnqsrLDALEKEVKKLGEEGAALR---GQLDALTKQLQRDESEAQSLRQEEQALTQQWQA---VCAS 587

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  747 LTAEKGQQGVGPPTDNEARELAAQLALS------QAQLEVHQGEVQRLQAQVVDLQAKMRAALD-------DQDKVQSQL 813
Cdd:PRK10246  588 LNITLQPQDDIQPWLDAQEEHERQLRLLsqrhelQGQIAAHNQQIIQYQQQIEQRQQQLLTALAgyaltlpQEDEEASWL 667

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  814 SMAEAvlrEHKTLVQQLKEQNEALNR-AHVQELLQCSEREGALQEERADEAQqreEELRALQEElsqakCSSEEAQLEHA 892
Cdd:PRK10246  668 ATRQQ---EAQSWQQRQNELTALQNRiQQLTPLLETLPQSDDLPHSEETVAL---DNWRQVHEQ-----CLSLHSQLQTL 736

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  893 ELQEQLHRANTDTAElgiqvcaltvekERVEEALACAVQELQDAKEAASREREGLERqvagLQQEKESLQEKLKAAKAaa 972
Cdd:PRK10246  737 QQQDVLEAQRLQKAQ------------AQFDTALQASVFDDQQAFLAALLDEETLTQ----LEQLKQNLENQRQQAQT-- 798

                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157738667  973 gslpgLQAQLAQAEQRAQSLQEAAHQELNTLKfQLSAEIMDYQSRLKNAGEECKSLRGQL--EEQGRQLQAA 1042
Cdd:PRK10246  799 -----LVTQTAQALAQHQQHRPDGLDLTVTVE-QIQQELAQLAQQLRENTTRQGEIRQQLkqDADNRQQQQA 864
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 590-900 2.23e-05

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 48.97  E-value: 2.23e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   590 EEQRGLQEAQlddtkvqEGSQEEELRQANRELEKELQNVVGRNQLLEGKLQALQADYQALQQRESAIQGS-LASLEAEQA 668
Cdd:pfam17380  313 ERRRKLEEAE-------KARQAEMDRQAAIYAEQERMAMERERELERIRQEERKRELERIRQEEIAMEISrMRELERLQM 385

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   669 SIRHLGDQMEASLLAVRKakeaMKAQMAEKEAILQSKEGECQQLREEVEqcqqlaEARHRELRALESQCQQQTQLIEVLT 748
Cdd:pfam17380  386 ERQQKNERVRQELEAARK----VKILEEERQRKIQQQKVEMEQIRAEQE------EARQREVRRLEEERAREMERVRLEE 455

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   749 AEKgQQGVGPPTDNEARELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQsqlsMAEAVLREHKTLVQ 828
Cdd:pfam17380  456 QER-QQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRK----LLEKEMEERQKAIY 530

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157738667   829 QLKEQNEAlnrahvqellqcseregalQEERadEAQQREEELRALQEELSQAkcSSEEAQLEHAELQEQLHR 900
Cdd:pfam17380  531 EEERRREA-------------------EEER--RKQQEMEERRRIQEQMRKA--TEERSRLEAMEREREMMR 579
HMMR_N pfam15905
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ...
 613-748 2.47e-05

Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.


Pssm-ID: 464932 [Multi-domain]  Cd Length: 329  Bit Score: 48.27  E-value: 2.47e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   613 ELRQANRELEKELQNVVGRNQLLEGKLQALQADYQALQQRESAIQGSLASLEAEQ--------------ASIRHLGDQME 678
Cdd:pfam15905  160 ELMKLRNKLEAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEKEKieekseteklleyiTELSCVSEQVE 239

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157738667   679 ASLLAVRKAKEAMKAQMAE----KEAILQSKEGECQQLREEVEQCQQLAEARHRELRALESQCQQQTQLIEVLT 748
Cdd:pfam15905  240 KYKLDIAQLEELLKEKNDEieslKQSLEEKEQELSKQIKDLNEKCKLLESEKEELLREYEEKEQTLNAELEELK 313
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 241-805 2.55e-05

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 49.20  E-value: 2.55e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   241 QLEVREKQLRERMQQLDRENQELRAAVSQQGE-QLQTERERGRTAAEDNVRL-----TCLVAELQKQWEVTQATQNTVKE 314
Cdd:TIGR00618  308 QAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSiEEQRRLLQTLHSQEIHIRDahevaTSIREISCQQHTLTQHIHTLQQQ 387

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   315 LQTCLQGLELGAAEKEEdyhtaLRRLESMLQPLAQELEATRDSLDKKNQHLASFPGWLAMAQQKADTASDTKGRQEPIPS 394
Cdd:TIGR00618  388 KTTLTQKLQSLCKELDI-----LQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQ 462

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   395 DAAQEMQELGEKLQALER-----ERTKVEEVNRQQSAQLEQLVKELQLKEDARAS-----LERLVKEMAPLQEELSGKGQ 464
Cdd:TIGR00618  463 ESAQSLKEREQQLQTKEQihlqeTRKKAVVLARLLELQEEPCPLCGSCIHPNPARqdidnPGPLTRRMQRGEQTYAQLET 542

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   465 EADQLWRRLQELLAHTSSWEEELAELRREKKQQQEEKELLEQEVRSLTRQLQFLETQLAQVSQH------VSDLEEQKKQ 538
Cdd:TIGR00618  543 SEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAedmlacEQHALLRKLQ 622

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   539 LIQDKDHLSQQVGMLER-----LAGPPGPELPVAGEKNEALVPVNSSLQEAWGkpeeEQRGLQEAQLDDTKVQEGSQEEE 613
Cdd:TIGR00618  623 PEQDLQDVRLHLQQCSQelalkLTALHALQLTLTQERVREHALSIRVLPKELL----ASRQLALQKMQSEKEQLTYWKEM 698

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   614 LRQANRELEKELQNVVGRNQLLEGKLQALQADYQALQQRESAIQGSLASLEAEQASirhlgdqmeasllaVRKAKEAMKA 693
Cdd:TIGR00618  699 LAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQART--------------VLKARTEAHF 764

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   694 QMAEKEAILQSKEGECQQLREEVEQCQQLAEARHRELRALESQCQQQT---QLIEVLTAEKGQQGVgPPTDNEARELAAQ 770
Cdd:TIGR00618  765 NNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIpsdEDILNLQCETLVQEE-EQFLSRLEEKSAT 843

                          570       580       590
                   ....*....|....*....|....*....|....*
gi 157738667   771 LALSQAQLEvHQGEVQRLQAQVVDLQAKMRAALDD 805
Cdd:TIGR00618  844 LGEITHQLL-KYEECSKQLAQLTQEQAKIIQLSDK 877
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 240-478 2.64e-05

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: 48.22  E-value: 2.64e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  240 DQLEVREKQLRERMQQLDRENQELRAAVSQQGEQLQterergrtaaednvrltclvaELQKQWEVTQATQNTVKELQTCL 319
Cdd:COG4942    20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLK---------------------QLAALERRIAALARRIRALEQEL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  320 QGLELGAAEKEEDYHTALRRLESMLQPLAQEL-EATRDSLDKKNQHLASFPGWLAMAQQKADTASDTKGRQEPIpSDAAQ 398
Cdd:COG4942    79 AALEAELAELEKEIAELRAELEAQKEELAELLrALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQA-EELRA 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  399 EMQELGEKLQALERERTKVEEVNRQQSAQLEQLVKELQLKEDARASLErlvKEMAPLQEELSGKGQEADQLWRRLQELLA 478
Cdd:COG4942   158 DLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLE---KELAELAAELAELQQEAEELEALIARLEA 234
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 395-730 2.79e-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: 49.18  E-value: 2.79e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  395 DAAQEMQELGEKLQALERERTKVEEVNRQQSAQLEQLVKELQLkedarasLERLVKEMAPLQEE-LSGKGQEADQLWRRL 473
Cdd:COG3096   833 DPEAELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQL-------LNKLLPQANLLADEtLADRLEELREELDAA 905

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  474 QELLAHTSSweeelaelrrekkqqqeekelLEQEVRSLTRQLQFLET---QLAQVSQHVSDLEEQKKQLIQDKDHLSQQV 550
Cdd:COG3096   906 QEAQAFIQQ---------------------HGKALAQLEPLVAVLQSdpeQFEQLQADYLQAKEQQRRLKQQIFALSEVV 964

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  551 GMLERLagppgpelpvAGEKNEALVPVNSSLQEAWgkpeeeqrglqEAQLDDTKVQEGSQEEELRQANRELEKELQnvvg 630
Cdd:COG3096   965 QRRPHF----------SYEDAVGLLGENSDLNEKL-----------RARLEQAEEARREAREQLRQAQAQYSQYNQ---- 1019

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  631 RNQLLEGKLQALQADYQALQQRESAIQGSLASLEAEQASIRHlgDQMEASLLAVRKAKEAMKAQMAEKEAILQSKEGEC- 709
Cdd:COG3096  1020 VLASLKSSRDAKQQTLQELEQELEELGVQADAEAEERARIRR--DELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLr 1097

                         330       340       350
                  ....*....|....*....|....*....|..
gi 157738667  710 ------QQLREEVEQ-----CQQLAEARHREL 730
Cdd:COG3096  1098 kaerdyKQEREQVVQakagwCAVLRLARDNDV 1129
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 609-1165 3.24e-05

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 48.48  E-value: 3.24e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   609 SQEEELRQANRELEKELQNVVGRNQLLEGKLQALQADYQALQQRESAIQGSLASLEAEQASIRHLGDQ---MEASLLAVR 685
Cdd:TIGR04523  152 KELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQiseLKKQNNQLK 231

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   686 KAKEAMKAQMAEKEAILQSKEGECQQLREE-------VEQCQQLAEARHRELRALESQCQQQTQLIEVLTAEKgQQGVGP 758
Cdd:TIGR04523  232 DNIEKKQQEINEKTTEISNTQTQLNQLKDEqnkikkqLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQK-EQDWNK 310

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   759 PTDNEARELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLsmaeavlREHKTLVQQLKEQNEALN 838
Cdd:TIGR04523  311 ELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQREL-------EEKQNEIEKLKKENQSYK 383

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   839 RAHVQELLQCSEREGALQEERaDEAQQREEELRALQEELsqakcssEEAQLEHAELQEQLHRANTDTAELgiqvcaltve 918
Cdd:TIGR04523  384 QEIKNLESQINDLESKIQNQE-KLNQQKDEQIKKLQQEK-------ELLEKEIERLKETIIKNNSEIKDL---------- 445

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   919 kERVEEALACAVQELQDAKEAASREREGLERQVAGLQQEKESLQEKLKAAKAAagsLPGLQAQLAQAEQRAQSLQE---- 994
Cdd:TIGR04523  446 -TNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKE---LKKLNEEKKELEEKVKDLTKkiss 521

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   995 --AAHQELNTLKFQLSAEIMDYQSRLKNAGEECKS--LRGQLEEQGRQLQAAEEAVEKLKATQADMGEKLSCTSNHLAEC 1070
Cdd:TIGR04523  522 lkEKIEKLESEKKEKESKISDLEDELNKDDFELKKenLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDL 601

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  1071 QAAMLRKDKEGAALREDLERTQKELEKATT---KIQEYYNKLCQEVTNRE---RNDQKMLADLDDLNRTKKYLEERLIEL 1144
Cdd:TIGR04523  602 IKEIEEKEKKISSLEKELEKAKKENEKLSSiikNIKSKKNKLKQEVKQIKetiKEIRNKWPEIIKKIKESKTKIDDIIEL 681

                          570       580
                   ....*....|....*....|.
gi 157738667  1145 LRDkdalWQKSDALEFQQKLS 1165
Cdd:TIGR04523  682 MKD----WLKELSLHYKKYIT 698
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
512-846 3.77e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 48.37  E-value: 3.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  512 TRQLQFLETQLAQVSQHVSDLEEQKKQLIQDKDHLSQQVGMLERLAGPPGPELPVAG------EKNEALVPVNSS----- 580
Cdd:COG4913   609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASaereiaELEAELERLDASsddla 688

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  581 -LQEAWGKPEEEQRGLQEaQLDDTKVQEGSQEEELRQANRELEKELQNVVGRNQLLE-GKLQALQADYQAL--QQRESAI 656
Cdd:COG4913   689 aLEEQLEELEAELEELEE-ELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARlELRALLEERFAAAlgDAVEREL 767

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  657 QGSL-ASLEAEQASIRHLGDQMEASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEveqcqQLAEARHRELRALES 735
Cdd:COG4913   768 RENLeERIDALRARLNRAEEELERAMRAFNREWPAETADLDADLESLPEYLALLDRLEED-----GLPEYEERFKELLNE 842

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  736 QCQQ-QTQLIEVLTAEKgqqgvgpptdNEARELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAkMRAALDDQDKVQSQLS 814
Cdd:COG4913   843 NSIEfVADLLSKLRRAI----------REIKERIDPLNDSLKRIPFGPGRYLRLEARPRPDPE-VREFRQELRAVTSGAS 911

                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 157738667  815 MAEAVLREH-----KTLVQQLKEQNEALNRAHVQELL 846
Cdd:COG4913   912 LFDEELSEArfaalKRLIERLRSEEEESDRRWRARVL 948
PRK10929 PRK10929
putative mechanosensitive channel protein; Provisional
 611-991 3.83e-05

putative mechanosensitive channel protein; Provisional


Pssm-ID: 236798 [Multi-domain]  Cd Length: 1109  Bit Score: 48.51  E-value: 3.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  611 EEELRQanrELeKELQNVVGRNQLleGKLQALQADYQALQQResaiQGSLASLEAEQASI-------RHLGDQMEASLLA 683
Cdd:PRK10929   25 EKQITQ---EL-EQAKAAKTPAQA--EIVEALQSALNWLEER----KGSLERAKQYQQVIdnfpklsAELRQQLNNERDE 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  684 VRKAKEAMKAQMAEKEaILQSKegecQQLREEVEQCQQLAEaRHRELRALESQC-QQQTQLIEVLT-AEKGQQGVGPPTD 761
Cdd:PRK10929   95 PRSVPPNMSTDALEQE-ILQVS----SQLLEKSRQAQQEQD-RAREISDSLSQLpQQQTEARRQLNeIERRLQTLGTPNT 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  762 nearelaaqlALSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEavlREHKTLVQQLKEQNEALNRAH 841
Cdd:PRK10929  169 ----------PLAQAQLTALQAESAALKALVDELELAQLSANNRQELARLRSELAK---KRSQQLDAYLQALRNQLNSQR 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  842 VQELLQCSEREGALQEERADEAQQREEELRaLQEELSQAkcSSEEAQlEHAELQEQLHRANTDTaelgIQV-CALTVEKE 920
Cdd:PRK10929  236 QREAERALESTELLAEQSGDLPKSIVAQFK-INRELSQA--LNQQAQ-RMDLIASQQRQAASQT----LQVrQALNTLRE 307

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  921 RVE---------EALACAVQELQDAKEAASREREGLERQVAGLQQEK--ESLQEKLKAAKAAAGSLPGLQAQLAQAEQRA 989
Cdd:PRK10929  308 QSQwlgvsnalgEALRAQVARLPEMPKPQQLDTEMAQLRVQRLRYEDllNKQPQLRQIRQADGQPLTAEQNRILDAQLRT 387


                  ..
gi 157738667  990 QS 991
Cdd:PRK10929  388 QR 389
COG3899 COG3899
Predicted ATPase [General function prediction only];
640-1096 4.56e-05

Predicted ATPase [General function prediction only];


Pssm-ID: 443106 [Multi-domain]  Cd Length: 1244  Bit Score: 48.32  E-value: 4.56e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  640 QALQADYQALQQRESAIQGSLASLEAEQASIRHLGDQMEASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEVEQC 719
Cdd:COG3899   770 RALAARALAALAALRHGNPPASARAYANLGLLLLGDYEEAYEFGELALALAERLGDRRLEARALFNLGFILHWLGPLREA 849

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  720 QQLAEARHRELRALESQCQQQTQLIEVLTAEKGQQGVGPPTDNEARELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKM 799
Cdd:COG3899   850 LELLREALEAGLETGDAALALLALAAAAAAAAAAAALAAAAAAAARLLAAAAAALAAAAAAAALAAAELARLAAAAAAAA 929

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  800 RAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNEALNRAHVQELLQCSEREGALQEERADEAQQREEELRALQEELSQ 879
Cdd:COG3899   930 ALALAAAAAAAAAAALAAAAAAAALAAALALAAAAAAAAAAALAAAAAAAAAAAAAAAAAALEAAAAALLALLAAAAAAA 1009

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  880 AkCSSEEAQLEHAELQEQLHRANTDTAELGIQVCALTVEKERVEEALACAVQELQDAKEAASREREGLERQVAGLQQEKE 959
Cdd:COG3899  1010 A-AAAALAAALLAAALAALAAAAAAAALLAAAAALALLAALAAAAAAAAAAAALAAAAALLAAAAAAAAAAAAAAAAAAL 1088

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  960 SLQEKLKAAKAAAGSLPGLQAQLAQAEQRAQSLQEAAHQELNTLKFQLSAEIMDYQSRLKNAGEECKSLRGQLEEQGRQL 1039
Cdd:COG3899  1089 AAALAAAALAAAAAAALALAAALAALALAAALAALALAAAARAAAALLLLAAALALALAALLLLAALLLALALLLLALAA 1168

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 157738667 1040 QAAEEAVEKLKATQADMGEKLSCTSNHLAECQAAMLRKDKEGAALREDLERTQKELE 1096
Cdd:COG3899  1169 LALAAALAALAAALLAAAAAAAAAAALLAALLALAARLAALLALALLALEAAALLLL 1225
DUF4686 pfam15742
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ...
 698-965 5.72e-05

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: 47.37  E-value: 5.72e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   698 KEAILQSKEGECQQLREEVEQCQQLAEARHRELRALESQCQQQTQLIEVLTAEKGQQGVgpptdnEARELAAQLALSQAQ 777
Cdd:pfam15742    4 GEKLKYQQQEEVQQLRQNLQRLQILCTSAEKELRYERGKNLDLKQHNSLLQEENIKIKA------ELKQAQQKLLDSTKM 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   778 LEVHQGEVQRLQAQVVDLQAKMraaLDDQDKVQSQLSMAEAVLREHKTLVQQLK---EQNEALNRAHVQELLQCSEREGA 854
Cdd:pfam15742   78 CSSLTAEWKHCQQKIRELELEV---LKQAQSIKSQNSLQEKLAQEKSRVADAEEkilELQQKLEHAHKVCLTDTCILEKK 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   855 LQEERADEAQQREEELRA-LQEELSQAKCSSEEAQlehaELQEQLhRANTDTAELGIQVCALTVEKERVEEALACAVQEL 933
Cdd:pfam15742  155 QLEERIKEASENEAKLKQqYQEEQQKRKLLDQNVN----ELQQQV-RSLQDKEAQLEMTNSQQQLRIQQQEAQLKQLENE 229

                          250       260       270
                   ....*....|....*....|....*....|..
gi 157738667   934 QDAKEAASREREGLERQVAGLQQEKESLQEKL 965
Cdd:pfam15742  230 KRKSDEHLKSNQELSEKLSSLQQEKEALQEEL 261
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
819-1159 6.26e-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: 6.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  819 VLREHKTL--VQQLKEQNEALNRAHvQELLQCSEREGALQ--EERADEAQQREEELRALQEELSQAKcsSEEAQLEHAEL 894
Cdd:COG4913   217 MLEEPDTFeaADALVEHFDDLERAH-EALEDAREQIELLEpiRELAERYAAARERLAELEYLRAALR--LWFAQRRLELL 293

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  895 QEQLHRantdtaelgiqvcaLTVEKERVEEALAcavqELQDAKEAASREREGLERQVAGLQ-QEKESLQEKLKaakaaag 973
Cdd:COG4913   294 EAELEE--------------LRAELARLEAELE----RLEARLDALREELDELEAQIRGNGgDRLEQLEREIE------- 348

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  974 slpGLQAQLAQAEQRAQSLQEAahqeLNTLKFQLSAEImdyqsrlknagEECKSLRGQLEEQGRQLQAAEEAVEKLKAtq 1053
Cdd:COG4913   349 ---RLERELEERERRRARLEAL----LAALGLPLPASA-----------EEFAALRAEAAALLEALEEELEALEEALA-- 408

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667 1054 admgeklsctsnhlaecqaamlrkdkegaalreDLERTQKELEKATTKIQeyynklcQEVTNRERN----DQKMLADLDD 1129
Cdd:COG4913   409 ---------------------------------EAEAALRDLRRELRELE-------AEIASLERRksniPARLLALRDA 448

                         330       340       350
                  ....*....|....*....|....*....|....*
gi 157738667 1130 LNRTKKYLEERL---IELL--RDKDALWQksDALE 1159
Cdd:COG4913   449 LAEALGLDEAELpfvGELIevRPEEERWR--GAIE 481
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 273-926 6.49e-05

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 47.51  E-value: 6.49e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   273 QLQTERERgrtAAEDNVRLTCLVAELQKQWEVTQATQNT----VKELQTCLQGLELGAAEKEED---------YHTALRR 339
Cdd:pfam10174  120 RLQSEHER---QAKELFLLRKTLEEMELRIETQKQTLGArdesIKKLLEMLQSKGLPKKSGEEDwertrriaeAEMQLGH 196

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   340 LESMLQPLAQELEATRDSLDKKNQhlasfpgwlamaqqkadtasdtkGRQEPIPSDAAQEMQELGE-KLQALERERTKVE 418
Cdd:pfam10174  197 LEVLLDQKEKENIHLREELHRRNQ-----------------------LQPDPAKTKALQTVIEMKDtKISSLERNIRDLE 253

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   419 -EVNRQQSAQL---EQLVKELQLKEDARASLERLVKEMAPLQEELSGKGQEADQLWRRLQELLAHTSSWEEELAELRREK 494
Cdd:pfam10174  254 dEVQMLKTNGLlhtEDREEEIKQMEVYKSHSKFMKNKIDQLKQELSKKESELLALQTKLETLTNQNSDCKQHIEVLKESL 333

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   495 KQQQEEKELLEQEVRSLTRQLQFLETQLAQVSQHVSDLEEQKKQLIQDKDHLSQQVGMLERlagppgpELPVAGEKNEAL 574
Cdd:pfam10174  334 TAKEQRAAILQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKER-------KINVLQKKIENL 406

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   575 VPVNSSLQEAWGKPEEEQRGLQ--------------EAQLDDTKVQEGSQEEELRQaNRELEKELQNVVGRNQLLEGKLQ 640
Cdd:pfam10174  407 QEQLRDKDKQLAGLKERVKSLQtdssntdtalttleEALSEKERIIERLKEQRERE-DRERLEELESLKKENKDLKEKVS 485

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   641 ALQADYQA-------LQQRESAIQGS-------LASLEAEQASIRHLGDQMEASLLAVRKAKEA--MKAQMAEKeaiLQS 704
Cdd:pfam10174  486 ALQPELTEkesslidLKEHASSLASSglkkdskLKSLEIAVEQKKEECSKLENQLKKAHNAEEAvrTNPEINDR---IRL 562

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   705 KEGECQQLREEVEQCQQLAEARHRELRALESQCQQQTQLIEVLTAEKGQQGVGPPTdnearelaaqlalSQAQLEVHQGE 784
Cdd:pfam10174  563 LEQEVARYKEESGKAQAEVERLLGILREVENEKNDKDKKIAELESLTLRQMKEQNK-------------KVANIKHGQQE 629

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   785 VQRLQAQVVDLQakmRAALDDQDKVQSQLSMAEAVLREHKTLvQQLKEQNEALnrAHVQELLQcsEREGALQEERADEAQ 864
Cdd:pfam10174  630 MKKKGAQLLEEA---RRREDNLADNSQQLQLEELMGALEKTR-QELDATKARL--SSTQQSLA--EKDGHLTNLRAERRK 701

                          650       660       670       680       690       700
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157738667   865 QREEELRALQEELsQAKCSSEEAQLEHAELQEQLHRANTDtaelgiQVCALTVEKERVEEAL 926
Cdd:pfam10174  702 QLEEILEMKQEAL-LAAISEKDANIALLELSSSKKKKTQE------EVMALKREKDRLVHQL 756
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 586-1154 6.95e-05

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 47.51  E-value: 6.95e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   586 GKPEEEQRGLQEAQLDDTKVQEGSQEEELRQANRELEKELQNVVGRNQLLEG--KLQALQADYQALQQRESAIQGSLASL 663
Cdd:pfam10174  173 PKKSGEEDWERTRRIAEAEMQLGHLEVLLDQKEKENIHLREELHRRNQLQPDpaKTKALQTVIEMKDTKISSLERNIRDL 252

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   664 EAEQASIRHLGD-----------QMEAsllaVRKAKEAMKAQMAEKEAILQSKEGE-----------------CQQ---- 711
Cdd:pfam10174  253 EDEVQMLKTNGLlhtedreeeikQMEV----YKSHSKFMKNKIDQLKQELSKKESEllalqtkletltnqnsdCKQhiev 328

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   712 LREEVEQCQQLAEARHRELRAL-------ESQCQQQTQLIEVLTAEKGQQGvgpptdNEARELAAQLALSQAQLEVHQGE 784
Cdd:pfam10174  329 LKESLTAKEQRAAILQTEVDALrlrleekESFLNKKTKQLQDLTEEKSTLA------GEIRDLKDMLDVKERKINVLQKK 402

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   785 VQRLQAQVVD-------LQAKMRAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNEALNRAHVQELlqcseregalqE 857
Cdd:pfam10174  403 IENLQEQLRDkdkqlagLKERVKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQREREDRERLEEL-----------E 471

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   858 ERADEAQQREEELRALQEELSQAKCSSEEAQLEHAELQEQLHRANTDTAELGIQVcaltveKERVEEALACAVQeLQDAK 937
Cdd:pfam10174  472 SLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAV------EQKKEECSKLENQ-LKKAH 544

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   938 EAASREREGLE--RQVAGLQQEKESLQEKlkaAKAAAGSLPGLQAQLAQAEQRA----------QSLQEAAHQELNTLKF 1005
Cdd:pfam10174  545 NAEEAVRTNPEinDRIRLLEQEVARYKEE---SGKAQAEVERLLGILREVENEKndkdkkiaelESLTLRQMKEQNKKVA 621

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  1006 QLSAeiMDYQSRLKNAGEECKSLRGQLEE----QGRQLQAAEEAVEKLKATQADMGEKLSCTSNHLAEcqaamlrKDKEG 1081
Cdd:pfam10174  622 NIKH--GQQEMKKKGAQLLEEARRREDNLadnsQQLQLEELMGALEKTRQELDATKARLSSTQQSLAE-------KDGHL 692

                          570       580       590       600       610       620       630
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157738667  1082 AALRedLERtQKELEKATTKIQEyynKLCQEVTNRERNdqkmLADLDDLNRTKKYLEERLIELLRDKDALWQK 1154
Cdd:pfam10174  693 TNLR--AER-RKQLEEILEMKQE---ALLAAISEKDAN----IALLELSSSKKKKTQEEVMALKREKDRLVHQ 755
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
236-805 8.27e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.22  E-value: 8.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  236 RLELDQLEVREKQLRERMQQLDRENQELRAAVSQQGEQLQTERERgrtaaednvrltclVAELQKQWEvtQATQNTVKEL 315
Cdd:COG4913   280 ALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREE--------------LDELEAQIR--GNGGDRLEQL 343

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  316 QTCLQGLELGAAEKE---EDYHTALRRLESMLQPLAQELEATRDSLDkknQHLASFPGWLAMAQQKADTASDTKgrqepi 392
Cdd:COG4913   344 EREIERLERELEERErrrARLEALLAALGLPLPASAEEFAALRAEAA---ALLEALEEELEALEEALAEAEAAL------ 414

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  393 pSDAAQEMQELGEKLQALERERTKVEEvnRQQSAqLEQLVKELQLKEDaraslerlvkEMAPLQEELSGKGQEADqlWRR 472
Cdd:COG4913   415 -RDLRRELRELEAEIASLERRKSNIPA--RLLAL-RDALAEALGLDEA----------ELPFVGELIEVRPEEER--WRG 478

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  473 LQELLAHTSSweeelaelrrekkqqqeekelleqevRSLtrqlqfL--ETQLAQVSQHVSDLeeqkkqliqdkdHLSQQV 550
Cdd:COG4913   479 AIERVLGGFA--------------------------LTL------LvpPEHYAAALRWVNRL------------HLRGRL 514

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  551 gMLERLAGPPGPELPVAGEKNE--ALVPVNSSLQEAWGKPEEEQRGL-----QEAQLDDTK---VQEG--SQEEELRQAN 618
Cdd:COG4913   515 -VYERVRTGLPDPERPRLDPDSlaGKLDFKPHPFRAWLEAELGRRFDyvcvdSPEELRRHPraiTRAGqvKGNGTRHEKD 593

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  619 RELEKELQNVVGRN-----QLLEGKLQALQADYQALQQRESAIQGSLASLEAEQASIRHLgDQMEASLLAVRKAKEAMKA 693
Cdd:COG4913   594 DRRRIRSRYVLGFDnraklAALEAELAELEEELAEAEERLEALEAELDALQERREALQRL-AEYSWDEIDVASAEREIAE 672

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  694 QMAEKEAILQSKeGECQQLREEVEQCQQLAEARHRELRALESQC----QQQTQLIEVLTAEKGQQGVGPPTDNEARELAA 769
Cdd:COG4913   673 LEAELERLDASS-DDLAALEEQLEELEAELEELEEELDELKGEIgrleKELEQAEEELDELQDRLEAAEDLARLELRALL 751

                         570       580       590
                  ....*....|....*....|....*....|....*..
gi 157738667  770 QLALSQAQLEVHQGEVQR-LQAQVVDLQAKMRAALDD 805
Cdd:COG4913   752 EERFAAALGDAVERELREnLEERIDALRARLNRAEEE 788
HCR pfam07111
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ...
 249-958 9.55e-05

Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.


Pssm-ID: 284517 [Multi-domain]  Cd Length: 749  Bit Score: 47.05  E-value: 9.55e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   249 LRERMQQLDRENQELRaavsQQGEQLQTERErgrTAAEDNVRLTCLVAELQKQWEVTQATQNTVKELQTCLQGLELGAAE 328
Cdd:pfam07111   61 LSQQAELISRQLQELR----RLEEEVRLLRE---TSLQQKMRLEAQAMELDALAVAEKAGQAEAEGLRAALAGAEMVRKN 133

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   329 KEEDYHTALRRLESMLQplaqeleatrdsldkknQHLASfpgwLAMAQQKA--DTASDTKGRQEPIPSdaaQEMQELGEK 406
Cdd:pfam07111  134 LEEGSQRELEEIQRLHQ-----------------EQLSS----LTQAHEEAlsSLTSKAEGLEKSLNS---LETKRAGEA 189

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   407 LQALERERtKVEEVNRQQSAQLEQLVKELQLKEdaraSLERLVKEMAPLQEELSGKGQEADQLWRRLQELlahtssweee 486
Cdd:pfam07111  190 KQLAEAQK-EAELLRKQLSKTQEELEAQVTLVE----SLRKYVGEQVPPEVHSQTWELERQELLDTMQHL---------- 254

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   487 laelRREKKQQQEEKELLEQEVRSLTRQLQFLETQLAQVSQHVSDLEEQ-----------------------KKQLIQDK 543
Cdd:pfam07111  255 ----QEDRADLQATVELLQVRVQSLTHMLALQEEELTRKIQPSDSLEPEfpkkcrsllnrwrekvfalmvqlKAQDLEHR 330

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   544 DHLSQQVGMLERLAgppgpELPVAGEKNEALvpVNSSLQEAWGKPEEEQRGLQEAQLDDTKVQEGSQEEELRQANreLEK 623
Cdd:pfam07111  331 DSVKQLRGQVAELQ-----EQVTSQSQEQAI--LQRALQDKAAEVEVERMSAKGLQMELSRAQEARRRQQQQTAS--AEE 401

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   624 ELQNVVGrnqllegklqalqadyqALQQRESAIQGSLASLEAEQASIRHLGDQMEaslLAVRKAkEAMKAQMAEKEAILQ 703
Cdd:pfam07111  402 QLKFVVN-----------------AMSSTQIWLETTMTRVEQAVARIPSLSNRLS---YAVRKV-HTIKGLMARKVALAQ 460

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   704 SKEGEC------QQLREEVE-QCQQLAEARHRelraLESQCQQQTQLIevltaekgQQGVGpptdnEARElaaqlalsqa 776
Cdd:pfam07111  461 LRQESCpppppaPPVDADLSlELEQLREERNR----LDAELQLSAHLI--------QQEVG-----RARE---------- 513

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   777 qlevhQGEVQRLQAQVVDLQAkmraaldDQDKVQSQLSMAEAVLREHKTLVQQLKEQNEALNRAhvQELLQCSEREGALQ 856
Cdd:pfam07111  514 -----QGEAERQQLSEVAQQL-------EQELQRAQESLASVGQQLEVARQGQQESTEEAASLR--QELTQQQEIYGQAL 579

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   857 EERADEAQQReeelraLQEELSQAKCSSEEAQLEHAE----LQEQLHRAntdtaelgiqvcalTVEKERVEEalacaVQE 932
Cdd:pfam07111  580 QEKVAEVETR------LREQLSDTKRRLNEARREQAKavvsLRQIQHRA--------------TQEKERNQE-----LRR 634

                          730       740
                   ....*....|....*....|....*.
gi 157738667   933 LQDakEAASREREGLERQVAGLQQEK 958
Cdd:pfam07111  635 LQD--EARKEEGQRLARRVQELERDK 658
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
376-822 1.12e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 46.68  E-value: 1.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  376 QQKADTASDTKGRQEPIPSDAAQEMQELGEKLQALERERTKVEEVNRQQSAQLEQLVKELQLKEDARASLERLV------ 449
Cdd:COG4717    52 EKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLqllply 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  450 KEMAPLQEELSGKGQEADQLWRRLQELLAHTSSWEEELAELRRE----KKQQQEEKELLEQEVRSLTRQLQFLETQLAQV 525
Cdd:COG4717   132 QELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELqeelEELLEQLSLATEEELQDLAEELEELQQRLAEL 211

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  526 SQHVSDLEEQKKQLIQDKDHLSQQ-------------------VGMLERLAGPPGPELPVAGEKNEALVPVNS--SLQEA 584
Cdd:COG4717   212 EEELEEAQEELEELEEELEQLENEleaaaleerlkearlllliAAALLALLGLGGSLLSLILTIAGVLFLVLGllALLFL 291

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  585 WGKPEEEQRGLQEAQLDDTKVQEGSQEEELRQANRELEKELQNVVGRNQLLEGKLQALQADYQALQQRESAIQgsLASLE 664
Cdd:COG4717   292 LLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQ--LEELE 369

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  665 AEQasirhlgdqmeASLLAvrkakeamKAQMAEKEailqskegecqQLREEVEQCQQLAEARhRELRALESQCQQQTQLI 744
Cdd:COG4717   370 QEI-----------AALLA--------EAGVEDEE-----------ELRAALEQAEEYQELK-EELEELEEQLEELLGEL 418

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  745 EVLTAekgqqgvgpptDNEARELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQ--DKVQSQLSMAEAVLRE 822
Cdd:COG4717   419 EELLE-----------ALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGelAELLQELEELKAELRE 487
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
856-1056 1.48e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 46.55  E-value: 1.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  856 QEERADEAQQReeeLRALQEELSQAKcsseeAQLEHAELQEQLHRANTDTAELGIQVCALTVEKERVEEALAcavqELQD 935
Cdd:COG3206   166 LELRREEARKA---LEFLEEQLPELR-----KELEEAEAALEEFRQKNGLVDLSEEAKLLLQQLSELESQLA----EARA 233

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  936 AKEAASREREGLERQVAGLQQEKESLQEklkaakaaAGSLPGLQAQLAQAEQRAQSLQE----------AAHQELNTLKF 1005
Cdd:COG3206   234 ELAEAEARLAALRAQLGSGPDALPELLQ--------SPVIQQLRAQLAELEAELAELSArytpnhpdviALRAQIAALRA 305

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 157738667 1006 QLSAEIMDYQSRLKNageECKSLRGQLEEQGRQLQAAEEAVEKLKATQADM 1056
Cdd:COG3206   306 QLQQEAQRILASLEA---ELEALQAREASLQAQLAQLEARLAELPELEAEL 353
PRK11281 PRK11281
mechanosensitive channel MscK;
596-878 1.80e-04

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 46.44  E-value: 1.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  596 QEAQLDDTKVQEGSQEEELRQANRELE--KELQNVVGRNQL-------LEGKLQALQADYQALQQRESAIQGSLASLEAe 666
Cdd:PRK11281   78 QKEETEQLKQQLAQAPAKLRQAQAELEalKDDNDEETRETLstlslrqLESRLAQTLDQLQNAQNDLAEYNSQLVSLQT- 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  667 qASIRhlgdqmeasllaVRKAKEAMKAQMAEKEAILQSKEGECQQLREEVeqcQQLAEArhrELRALESQCQQQTQLIEV 746
Cdd:PRK11281  157 -QPER------------AQAALYANSQRLQQIRNLLKGGKVGGKALRPSQ---RVLLQA---EQALLNAQNDLQRKSLEG 217

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  747 LTaekgqqgvgpptdnearelaaQL-ALSQAQLEVHQGEVQRLQAQVVDLQakmrAALDDQDKVQSQLSMAEAVLREHKT 825
Cdd:PRK11281  218 NT---------------------QLqDLLQKQRDYLTARIQRLEHQLQLLQ----EAINSKRLTLSEKTVQEAQSQDEAA 272

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157738667  826 LVQQ--LKEQNEALNRAHVQELLQCSEREGAL--QEERA----DEAQQREeelRALQEELS 878
Cdd:PRK11281  273 RIQAnpLVAQELEINLQLSQRLLKATEKLNTLtqQNLRVknwlDRLTQSE---RNIKEQIS 330
HMMR_N pfam15905
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ...
 795-965 1.85e-04

Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.


Pssm-ID: 464932 [Multi-domain]  Cd Length: 329  Bit Score: 45.57  E-value: 1.85e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   795 LQAKMRAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNEALNRAHVQELLQcseregalqeeradeaqqrEEELRALQ 874
Cdd:pfam15905  168 LEAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEKEKIEEKSE-------------------TEKLLEYI 228

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   875 EELSQAKCSSEEAQLEHAELQEQLHRANTDTAELGIQVCALTVEKERVEEALACAVQELQDAKEAASREREGLERqvaGL 954
Cdd:pfam15905  229 TELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELSKQIKDLNEKCKLLESEKEELLREYEEKEQ---TL 305

                          170
                   ....*....|.
gi 157738667   955 QQEKESLQEKL 965
Cdd:pfam15905  306 NAELEELKEKL 316
PRK11281 PRK11281
mechanosensitive channel MscK;
640-904 2.58e-04

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 45.67  E-value: 2.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  640 QALQADYQALQQRESaiqgslasLEAEQASIRHLGDQMEASLlavrKAKEAMKAQMAEKEAILQSKEGECQQLREEVEQC 719
Cdd:PRK11281   39 ADVQAQLDALNKQKL--------LEAEDKLVQQDLEQTLALL----DKIDRQKEETEQLKQQLAQAPAKLRQAQAELEAL 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  720 QQLAEARHRELRALESQCQQQTQLIEVLTAEKGQQgvgpptdNEARELAAQLALSQAQLEVHQGE----VQRLQ---AQV 792
Cdd:PRK11281  107 KDDNDEETRETLSTLSLRQLESRLAQTLDQLQNAQ-------NDLAEYNSQLVSLQTQPERAQAAlyanSQRLQqirNLL 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  793 VDLQAKMRAALDDQ-DKVQSQLSMAEAVLRehktLVQQLKEQNEALnrahvQELLQcSEREgalqeERADEAQQREEELR 871
Cdd:PRK11281  180 KGGKVGGKALRPSQrVLLQAEQALLNAQND----LQRKSLEGNTQL-----QDLLQ-KQRD-----YLTARIQRLEHQLQ 244

                         250       260       270
                  ....*....|....*....|....*....|...
gi 157738667  872 ALQEELSQAKCSSEEAQLEHAELQEQLHRANTD 904
Cdd:PRK11281  245 LLQEAINSKRLTLSEKTVQEAQSQDEAARIQAN 277
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
250-451 3.04e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 45.68  E-value: 3.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  250 RERMQQLDRENQELRAAVSQQGEQLQTERERGRTAAEdnvRLTCLVAELQKQWEV--TQATQNTVKELQTCLQGLELGAA 327
Cdd:COG4913   609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQE---RREALQRLAEYSWDEidVASAEREIAELEAELERLDASSD 685

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  328 EkeedyhtaLRRLESMLQPLAQELEATRDSLDKKNQHLASFPGWLAMAQQKADTASDtkgRQEPIPSDAAQEMQELGEKL 407
Cdd:COG4913   686 D--------LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQD---RLEAAEDLARLELRALLEER 754

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 157738667  408 QALERERTKVEEVNRQQSAQLEQLVKELqlkEDARASLERLVKE 451
Cdd:COG4913   755 FAAALGDAVERELRENLEERIDALRARL---NRAEEELERAMRA 795
FYVE_RUFY3 cd15744
FYVE-related domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar ...
 1179-1227 3.04e-04

FYVE-related domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar proteins; RUFY3, also termed 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. Moreover, the FYVE domain of RUFY3 resembles the FYVE-related domain as it lacks the WxxD motif (x for any residue).


Pssm-ID: 277283 [Multi-domain]  Cd Length: 52  Bit Score: 40.09  E-value: 3.04e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 157738667 1179 CLDCKREFSWMVR-RHHCRICGRIFCYYCCNNYV-LSKHGGKKERCCRACF 1227
Cdd:cd15744     2 CSLCQEDFASLALpKHNCYNCGGTFCDACSSNELpLPSSIYEPARVCDVCY 52
PRK11281 PRK11281
mechanosensitive channel MscK;
867-1118 3.16e-04

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 45.29  E-value: 3.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  867 EEELRALQEELSQAKCSSEEAQLEHAELQEQLhrantdtaelgiqvcALTVEKERVEEALACAVQELQDAKEAASREREG 946
Cdd:PRK11281   38 EADVQAQLDALNKQKLLEAEDKLVQQDLEQTL---------------ALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAE 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  947 LERQVAGLQQEKESLQEKLkaakaaagSLPGLQAQLAQAEQRAQSLQEAahqeLNTLKFQLSAeimdYQSRLKNAGEECK 1026
Cdd:PRK11281  103 LEALKDDNDEETRETLSTL--------SLRQLESRLAQTLDQLQNAQND----LAEYNSQLVS----LQTQPERAQAALY 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667 1027 SLRGQLEEQGRQLQAAEEAVEKLKATQADMGEklscTSNHLAECQAAMLRKDKEGAALREDLERTQKELEKATTKIQEYY 1106
Cdd:PRK11281  167 ANSQRLQQIRNLLKGGKVGGKALRPSQRVLLQ----AEQALLNAQNDLQRKSLEGNTQLQDLLQKQRDYLTARIQRLEHQ 242

                         250
                  ....*....|..
gi 157738667 1107 NKLCQEVTNRER 1118
Cdd:PRK11281  243 LQLLQEAINSKR 254
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
942-1125 3.33e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.14  E-value: 3.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  942 REREGLERQVAGLQQEKESLQEKLKAAKAAAGSLPGLQAQLAQAEQRAQSLQEA-AHQELNTLKFQLSAEIMDYQSRLKN 1020
Cdd:COG4717    71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLlQLLPLYQELEALEAELAELPERLEE 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667 1021 AGEECKSLRGQLEEQGRQLQAAEEAVEKLKATQADMGEKlscTSNHLAECQAAMLRKDKEGAALREDLERTQKELEKATT 1100
Cdd:COG4717   151 LEERLEELRELEEELEELEAELAELQEELEELLEQLSLA---TEEELQDLAEELEELQQRLAELEEELEEAQEELEELEE 227

                         170       180
                  ....*....|....*....|....*
gi 157738667 1101 KIQEYYNKLCQEVTNRERNDQKMLA 1125
Cdd:COG4717   228 ELEQLENELEAAALEERLKEARLLL 252
RecN COG0497
DNA repair ATPase RecN [Replication, recombination and repair];
765-1005 3.52e-04

DNA repair ATPase RecN [Replication, recombination and repair];


Pssm-ID: 440263 [Multi-domain]  Cd Length: 555  Bit Score: 45.07  E-value: 3.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  765 RELAAQLalsqaqLEVH-QGEVQRLqaqvvdLQAKM-RAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQnealnrahv 842
Cdd:COG0497   119 RELGELL------VDIHgQHEHQSL------LDPDAqRELLDAFAGLEELLEEYREAYRAWRALKKELEEL--------- 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  843 qellqcseregalqEERADEAQQREEELRALQEELSQAKCSS-EEAQLE-------HAE-LQEQLHRA------NTDTAE 907
Cdd:COG0497   178 --------------RADEAERARELDLLRFQLEELEAAALQPgEEEELEeerrrlsNAEkLREALQEAlealsgGEGGAL 243

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  908 LGIQVCALTVEK------------ERVEEALAcavqELQDAKEAASREREGLE------------------------RQV 951
Cdd:COG0497   244 DLLGQALRALERlaeydpslaelaERLESALI----ELEEAASELRRYLDSLEfdperleeveerlallrrlarkygVTV 319

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157738667  952 AGLQQEKESLQEKLKAAKAAAGSLPGLQAQLAQAEQR---------------AQSLQEAAHQELNTLKF 1005
Cdd:COG0497   320 EELLAYAEELRAELAELENSDERLEELEAELAEAEAElleaaeklsaarkkaAKKLEKAVTAELADLGM 388
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 789-951 3.82e-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: 43.76  E-value: 3.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  789 QAQVVDLQAkmraaLDDQ-DKVQSQLSMAEAVLREHKTLVQQLKEQNEALNRAHVQELLQCSEREGALQEERA----DEA 863
Cdd:COG1579     6 LRALLDLQE-----LDSElDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEArikkYEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  864 QQRE----EELRALQEELSQAKCSSEEAQLEHAELQEQLHRANTDTAELGIQVCALTVEKERVEEALACAVQELQDAKEA 939
Cdd:COG1579    81 QLGNvrnnKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEE 160

                         170
                  ....*....|..
gi 157738667  940 ASREREGLERQV 951
Cdd:COG1579   161 LEAEREELAAKI 172
FYVE_FGD3 cd15740
FYVE-like domain found in FYVE, RhoGEF and PH domain-containing protein 3 (FGD3) and similar ...
 1173-1227 4.28e-04

FYVE-like domain found in FYVE, RhoGEF and PH domain-containing protein 3 (FGD3) and similar proteins; FGD3, also termed zinc finger FYVE domain-containing protein 5, is a putative Cdc42-specific guanine nucleotide exchange factor (GEF) that undergoes the ubiquitin ligase SCFFWD1/beta-TrCP-mediated proteasomal degradation. It is a homologue of FGD1 and contains a DBL homology (DH) domain and pleckstrin homology (PH) domain in the middle region, a FYVE domain, and another PH domain in the C-terminus, but lacks the N-terminal proline-rich domain (PRD) found in FGD1. Due to this difference, FGD3 may play different roles from that of FGD1 to regulate cell morphology or motility. The FYVE domain of FGD3 resembles a FYVE-like domain that is different from the canonical FYVE domains, since it lacks one of the three conserved signature motifs (the WxxD motif) that are involved in phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) binding and exhibits altered lipid binding specificities.


Pssm-ID: 277279 [Multi-domain]  Cd Length: 54  Bit Score: 39.60  E-value: 4.28e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 157738667 1173 DTEANHCLDCKREFSWMV-RRHHCRICGRIFCYYCCNnyvLSKHGGKKERCCRACF 1227
Cdd:cd15740     2 EKEKQTCKGCNESFNSITkRRHHCKQCGAVICGKCSE---FKDLASRHNRVCRDCF 54
46 PHA02562
endonuclease subunit; Provisional
 593-814 4.48e-04

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 44.62  E-value: 4.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  593 RGLQEaQLDDTKVQEGSQEEELRQANReLEKELQNVVGRNqllegkLQALQADYQALQQRESAIQGSLASLEAEQASIRH 672
Cdd:PHA02562  177 RELNQ-QIQTLDMKIDHIQQQIKTYNK-NIEEQRKKNGEN------IARKQNKYDELVEEAKTIKAEIEELTDELLNLVM 248

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  673 LGDQMEASLLAVRKAKEAMKAQMA--EKEAILQSKEGEC----QQLREEVEQC----QQLAEARHRELRALESQCQQQTQ 742
Cdd:PHA02562  249 DIEDPSAALNKLNTAAAKIKSKIEqfQKVIKMYEKGGVCptctQQISEGPDRItkikDKLKELQHSLEKLDTAIDELEEI 328

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157738667  743 LIEVLTAEKGQQGVgpptDNEARELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLS 814
Cdd:PHA02562  329 MDEFNEQSKKLLEL----KNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKS 396
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 649-1176 4.94e-04

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 44.81  E-value: 4.94e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   649 LQQRESAIQGSLASLEAEQASIRHLGDQMEASLLAVRKAKE--AMKAQMAEK-------EAILQSKEGECQQLREEV--- 716
Cdd:pfam10174  139 LEEMELRIETQKQTLGARDESIKKLLEMLQSKGLPKKSGEEdwERTRRIAEAemqlghlEVLLDQKEKENIHLREELhrr 218

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   717 ----------EQCQQLAEARHRELRALESQCQQQTQLIEVLTAEkgqqGVGPPTDNEARELAAQLALSQA-----QLEVH 781
Cdd:pfam10174  219 nqlqpdpaktKALQTVIEMKDTKISSLERNIRDLEDEVQMLKTN----GLLHTEDREEEIKQMEVYKSHSkfmknKIDQL 294

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   782 QGEVQRLQAQVVDLQAKmraaLDDQDKVQSQLSMAEAVLREHKTlvqqLKEQNEALNRAHVQELLQCSEREGALQEERAD 861
Cdd:pfam10174  295 KQELSKKESELLALQTK----LETLTNQNSDCKQHIEVLKESLT----AKEQRAAILQTEVDALRLRLEEKESFLNKKTK 366

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   862 EAQQREEELRALQEELS----------------QAKCSSEEAQLEH-----AELQE-----QLHRANTDTAeLGIQVCAL 915
Cdd:pfam10174  367 QLQDLTEEKSTLAGEIRdlkdmldvkerkinvlQKKIENLQEQLRDkdkqlAGLKErvkslQTDSSNTDTA-LTTLEEAL 445

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   916 TvEKERVEEALacavqelqdaKEAASREREGLERQVAGLQQEKESLQEKLKAakaaagslpgLQAQLAQAEQRAQSLQEA 995
Cdd:pfam10174  446 S-EKERIIERL----------KEQREREDRERLEELESLKKENKDLKEKVSA----------LQPELTEKESSLIDLKEH 504

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   996 AhQELNTLKFQLSAEIMDYQSRLKNAGEECKSLRGQL---EEQGRQLQAAEEAVEKLKATQADMGEKLSCTSNHLAECQA 1072
Cdd:pfam10174  505 A-SSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLkkaHNAEEAVRTNPEINDRIRLLEQEVARYKEESGKAQAEVER 583

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  1073 AM--LR--------KDKEGAALREDLERTQKELEKATTKIqeyynKLCQEVTNRERNDQKMLADLDDLNRTKKYLEERLI 1142
Cdd:pfam10174  584 LLgiLRevenekndKDKKIAELESLTLRQMKEQNKKVANI-----KHGQQEMKKKGAQLLEEARRREDNLADNSQQLQLE 658

                          570       580       590
                   ....*....|....*....|....*....|....
gi 157738667  1143 ELLRDKDALWQKSDALefQQKLSAEERWLGDTEA 1176
Cdd:pfam10174  659 ELMGALEKTRQELDAT--KARLSSTQQSLAEKDG 690
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 829-1169 4.95e-04

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: 44.73  E-value: 4.95e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   829 QLKEQNEALNrahvqELLQCSEREGALQEERADEAQQREEELRALQEELSQAKCSSEEAQLEHAELQEQlhrantdtAEL 908
Cdd:pfam17380  263 QTMTENEFLN-----QLLHIVQHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQ--------AEM 329

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   909 GIQVcALTVEKERVeealacavqelqdakeAASREREgLER-QVAGLQQEKESL-QEKLKAAKAAAGSLPGLQAQLAQAE 986
Cdd:pfam17380  330 DRQA-AIYAEQERM----------------AMERERE-LERiRQEERKRELERIrQEEIAMEISRMRELERLQMERQQKN 391

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   987 QRAQSLQEAAHqelntlKFQLSAEimDYQSRLKNAGEECKSLRGQLEE-QGRQLQAAEEA----VEKLKATQADMGEKLS 1061
Cdd:pfam17380  392 ERVRQELEAAR------KVKILEE--ERQRKIQQQKVEMEQIRAEQEEaRQREVRRLEEErareMERVRLEEQERQQQVE 463

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  1062 CTSNHLAECQAAMLRKDKEgaalredlERTQKELEKATTKIQEYYNKLCQEVTNRERNDQKMLADLDDLNRTKKYLEE-- 1139
Cdd:pfam17380  464 RLRQQEEERKRKKLELEKE--------KRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEErr 535

                          330       340       350
                   ....*....|....*....|....*....|
gi 157738667  1140 RLIELLRDKDALWQKSDALEFQQKLSAEER 1169
Cdd:pfam17380  536 REAEEERRKQQEMEERRRIQEQMRKATEER 565
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 226-933 5.57e-04

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: 44.56  E-value: 5.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  226 NEALEGFDEMRLELDQLEVREKQLRERMQQLDRENQelraaVSQQGEQLQTERERGRTAAEDnvrltclVAELQKQWEVT 305
Cdd:COG3096   498 RELLRRYRSQQALAQRLQQLRAQLAELEQRLRQQQN-----AERLLEEFCQRIGQQLDAAEE-------LEELLAELEAQ 565

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  306 QATqntvkelqtclqgLELGAAEKEEDyHTALRRLESMLQPLAQELEATRdsldkknqhlasfPGWLAmAQQKADTASDT 385
Cdd:COG3096   566 LEE-------------LEEQAAEAVEQ-RSELRQQLEQLRARIKELAARA-------------PAWLA-AQDALERLREQ 617

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  386 KGRQEPIPSDAAQEMQELGEKLQALERERTKVEEVNRQQSAQLEQLVKE--------LQLKEDARASL-----ERLVKEM 452
Cdd:COG3096   618 SGEALADSQEVTAAMQQLLEREREATVERDELAARKQALESQIERLSQPggaedprlLALAERLGGVLlseiyDDVTLED 697

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  453 APLQEELSGKGQEA---DQLWRRLQELLAHTSS----WEEELAELRREKKQQQEEKELLEQEVRSLTRQLQ---FLETQL 522
Cdd:COG3096   698 APYFSALYGPARHAivvPDLSAVKEQLAGLEDCpedlYLIEGDPDSFDDSVFDAEELEDAVVVKLSDRQWRysrFPEVPL 777

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  523 ---AQVSQHVSDLEEQKKQLIQDKDHLSQQVGMLERLAgppgpelpvagEKNEALvpVNSSLQEAW-GKPEEEQRGLQE- 597
Cdd:COG3096   778 fgrAAREKRLEELRAERDELAEQYAKASFDVQKLQRLH-----------QAFSQF--VGGHLAVAFaPDPEAELAALRQr 844

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  598 -AQLDDTKVQEGSQEEELRQANRELEKELQNVvgrNQLLegKLQALQADyQALQQRESAIQGSLASLEAEQASIRHLGDQ 676
Cdd:COG3096   845 rSELERELAQHRAQEQQLRQQLDQLKEQLQLL---NKLL--PQANLLAD-ETLADRLEELREELDAAQEAQAFIQQHGKA 918

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  677 MEasllavrkakeamkaQMAEKEAILQSKEGECQQLREEVEQCQQlaearhrELRALESQCQQQTQLIEVLTAEKGQQGV 756
Cdd:COG3096   919 LA---------------QLEPLVAVLQSDPEQFEQLQADYLQAKE-------QQRRLKQQIFALSEVVQRRPHFSYEDAV 976

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  757 GppTDNEARELAAQLalsQAQLEvhQGEVQRLQAQVvdlqaKMRAAlddqdkvQSQLSMAEAVLRE----HKTLVQQLKE 832
Cdd:COG3096   977 G--LLGENSDLNEKL---RARLE--QAEEARREARE-----QLRQA-------QAQYSQYNQVLASlkssRDAKQQTLQE 1037

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  833 QNealnrahvQELLQCSEREGALQEERA-DEAQQREEELRALQEELSQAKCSSEEAQLEHAELQEQLHRANTDtaelgiq 911
Cdd:COG3096  1038 LE--------QELEELGVQADAEAEERArIRRDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERD------- 1102

                         730       740
                  ....*....|....*....|....
gi 157738667  912 vcaLTVEKERVEEALA--CAVQEL 933
Cdd:COG3096  1103 ---YKQEREQVVQAKAgwCAVLRL 1123
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
933-1131 5.61e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 44.62  E-value: 5.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  933 LQDAKEAASREREGLERQVAGLQQEKESLQEKLKAAKAAAG--SLPG------------------LQAQLAQAEQRAQSL 992
Cdd:COG3206   166 LELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGlvDLSEeaklllqqlselesqlaeARAELAEAEARLAAL 245

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  993 QEAAHQELNTLKFQL-SAEIMDYQSRLKNAGEECKSLRGQLEEQGRQLQAAEEAVEKLKATQADMGEKLsctsnhLAECQ 1071
Cdd:COG3206   246 RAQLGSGPDALPELLqSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRI------LASLE 319

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667 1072 AAMLRKDKEGAALREDLERTQKELEKATTKIQEyYNKLCQEVTNRERNDQKMLADLDDLN 1131
Cdd:COG3206   320 AELEALQAREASLQAQLAQLEARLAELPELEAE-LRRLEREVEVARELYESLLQRLEEAR 378
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 770-996 7.83e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 43.67  E-value: 7.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  770 QLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAvlrEHKTLVQQLKEQNEALNRAhvQELLqcs 849
Cdd:COG3883    17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQA---EIDKLQAEIAEAEAEIEER--REEL--- 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  850 eregalqEERADEAQQREEELRALQEELSQakcSSEEAQLEHAELQEQLHRANTDTAElgiQVCALTVEKERVEEALACA 929
Cdd:COG3883    89 -------GERARALYRSGGSVSYLDVLLGS---ESFSDFLDRLSALSKIADADADLLE---ELKADKAELEAKKAELEAK 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157738667  930 VQELQDAKEAASREREGLERQVAGLQQEKESLQEKLKAAKAAAGSLPGLQAQLAQAEQRAQSLQEAA 996
Cdd:COG3883   156 LAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAA 222
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 588-745 8.10e-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: 42.60  E-value: 8.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  588 PEEEQRGLQEAQLDDTKVQEgsqeeeLRQANRELEKELQNvvgrnqlLEGKLQALQADYQALQQRESAIQGSLASLEAEQ 667
Cdd:COG1579     2 MPEDLRALLDLQELDSELDR------LEHRLKELPAELAE-------LEDELAALEARLEAAKTELEDLEKEIKRLELEI 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  668 ASIRHLGDQMEASLLAVRKAKE---------AMKAQMAEKEAILQSKEGECQQLREEVEQCQQLAEARHRELRALESQCQ 738
Cdd:COG1579    69 EEVEARIKKYEEQLGNVRNNKEyealqkeieSLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELD 148


                  ....*..
gi 157738667  739 QQTQLIE 745
Cdd:COG1579   149 EELAELE 155
PRK12704 PRK12704
phosphodiesterase; Provisional
 979-1112 8.15e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 43.61  E-value: 8.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  979 QAQLAQAEQRAQSLQEAAHQELNTLKFQLSAEIMDYQSRLKNAGE-ECKSLRGQLEEQGRQLQAAEEAVEKLKatqadmg 1057
Cdd:PRK12704   30 EAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEkELRERRNELQKLEKRLLQKEENLDRKL------- 102

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 157738667 1058 EKLSctsnhlaecqaamlRKDKEGAALREDLERTQKELEKATTKIQEYYNKLCQE 1112
Cdd:PRK12704  103 ELLE--------------KREEELEKKEKELEQKQQELEKKEEELEELIEEQLQE 143
GOLD_2 pfam13897
Golgi-dynamics membrane-trafficking; Sec14-like Golgi-trafficking domain The GOLD domain is ...
 1419-1464 8.56e-04

Golgi-dynamics membrane-trafficking; Sec14-like Golgi-trafficking domain The GOLD domain is always found combined with lipid- or membrane-association domains.


Pssm-ID: 464028  Cd Length: 133  Bit Score: 40.93  E-value: 8.56e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 157738667  1419 LIPTTRCNSHKENIQGQLKVRTPGIYMLIFDNTFSRFVSKKVFYHL 1464
Cdd:pfam13897   85 IVPVYRRDCHEEVYAGSHQYPGRGVYLLKFDNSYSLWRSKTLYYRV 130
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 766-936 9.33e-04

Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.


Pssm-ID: 439154 [Multi-domain]  Cd Length: 309  Bit Score: 43.13  E-value: 9.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  766 ELAAQLALSQAQLEVhQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAVLREHKTLVQQLK--------EQNEAL 837
Cdd:cd22656    98 ELIDDLADATDDEEL-EEAKKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTALETLEkalkdlltDEGGAI 176

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  838 NRAHVQELLQcseregALQEERADEAQQREEELRALQEELsqakcSSEEAQLEHAE-LQEQLHRANTDTAELgiqvcalt 916
Cdd:cd22656   177 ARKEIKDLQK------ELEKLNEEYAAKLKAKIDELKALI-----ADDEAKLAAALrLIADLTAADTDLDNL-------- 237

                         170       180
                  ....*....|....*....|
gi 157738667  917 veKERVEEALAcAVQELQDA 936
Cdd:cd22656   238 --LALIGPAIP-ALEKLQGA 254
CHASE3 COG5278
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
588-1010 1.08e-03

Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];


Pssm-ID: 444089 [Multi-domain]  Cd Length: 530  Bit Score: 43.36  E-value: 1.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  588 PEEEQRGLQEAQLDDTKVQEGSQEEELRQAN-----RELEKELQNVVGRNQLLEGKLQALQADYQALQQRESAIQGSLAS 662
Cdd:COG5278   103 PEQQARLDELEALIDQWLAELEQVIALRRAGgleaaLALVRSGEGKALMDEIRARLLLLALALAALLLAAAALLLLLLAL 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  663 LEAEQASIRHLGDQMEASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEVEQCQQLAEARHRELRALESQCQQQTQ 742
Cdd:COG5278   183 AALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALALLLAALLLALLAALALAAL 262

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  743 LIEVLTAEKGQQGVGPPTDNEARELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAVLRE 822
Cdd:COG5278   263 LAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAAALAALLALALATALAAAAA 342

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  823 HKTLVQQLKEQNEALNRAHVQELLQCSEREGALQEERADEAQQREEELRALQEELSQAKCSSEEAQLEHAELQEQLHRAN 902
Cdd:COG5278   343 ALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAAAAEAAAAAAAAAAASAAEAL 422

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  903 TDTAELGIQVCALTVEKERVEEALACAVQELQDAKEAASREREGLERQVAGLQQEKESLQEKLKAAKAAAGSLPGLQAQL 982
Cdd:COG5278   423 ELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAAALAEAEAAAALAAAAALSLA 502

                         410       420
                  ....*....|....*....|....*...
gi 157738667  983 AQAEQRAQSLQEAAHQELNTLKFQLSAE 1010
Cdd:COG5278   503 LALAALLLAAAEAALAAALAAALASAEL 530
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
510-670 1.09e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 43.47  E-value: 1.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  510 SLTRQLQFLETQLAQVSQHVSDLEEQKKQLIQDKDHLSQQVGMlerlagppgpelpvaGEKNEALVPVNSSLQEAwgkpe 589
Cdd:COG3206   209 DLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGS---------------GPDALPELLQSPVIQQL----- 268

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  590 EEQRGLQEAQLDDTKVQEGSQEEELRQANRELEKELQNVvgrNQLLEGKLQALQADYQALQQRESAIQGSLASLEAEQAS 669
Cdd:COG3206   269 RAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQL---QQEAQRILASLEAELEALQAREASLQAQLAQLEARLAE 345


                  .
gi 157738667  670 I 670
Cdd:COG3206   346 L 346
PRK10246 PRK10246
exonuclease subunit SbcC; Provisional
 700-1049 1.10e-03

exonuclease subunit SbcC; Provisional


Pssm-ID: 182330 [Multi-domain]  Cd Length: 1047  Bit Score: 43.64  E-value: 1.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  700 AILQSKEGECQQLREEVE------QCQQLAEARHRELRALESQCQQQTQLIEVLTAEKGQQ---GVGPPTDNEARELAAQ 770
Cdd:PRK10246  160 AFLNAKPKERAELLEELTgteiygQISAMVFEQHKSARTELEKLQAQASGVALLTPEQVQSltaSLQVLTDEEKQLLTAQ 239

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  771 LALSQA-QLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAE--AVLR-------EHKTLVQQLKEQNEALN-R 839
Cdd:PRK10246  240 QQQQQSlNWLTRLDELQQEASRRQQALQQALAAEEKAQPQLAALSLAQpaRQLRphweriqEQSAALAHTRQQIEEVNtR 319

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  840 AHVQELLQCSEREGALQEERADEAQQRE--------EELRALQEELSQAKCSSEEAQLEHAELQEQLHRANTDTAEL-GI 910
Cdd:PRK10246  320 LQSTMALRARIRHHAAKQSAELQAQQQSlntwlaehDRFRQWNNELAGWRAQFSQQTSDREQLRQWQQQLTHAEQKLnAL 399

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  911 QVCALTVEKERVEEALAcavqelQDAKEAASRER-EGLERQVAGLQQEKESLQEKLKAAKAAAGSLPGLQAQLAQ----- 984
Cdd:PRK10246  400 PAITLTLTADEVAAALA------QHAEQRPLRQRlVALHGQIVPQQKRLAQLQVAIQNVTQEQTQRNAALNEMRQrykek 473

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  985 ----AEQRAQSLQEAAHQELNTLKFQLSA---------------------EIMDYQSRL-------KNAGEECKSLRGQL 1032
Cdd:PRK10246  474 tqqlADVKTICEQEARIKDLEAQRAQLQAgqpcplcgstshpaveayqalEPGVNQSRLdalekevKKLGEEGAALRGQL 553

                         410
                  ....*....|....*..
gi 157738667 1033 EEQGRQLQAAEEAVEKL 1049
Cdd:PRK10246  554 DALTKQLQRDESEAQSL 570
Golgin_A5 pfam09787
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ...
 701-908 1.10e-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: 42.82  E-value: 1.10e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   701 ILQSKEGECQQLRE---------------EVEQCQQLAEARHRELRALESQCQQ-QTQLIEVltaEKGQQgvgpptdNEA 764
Cdd:pfam09787   19 ILQSKEKLIASLKEgsgvegldsstaltlELEELRQERDLLREEIQKLRGQIQQlRTELQEL---EAQQQ-------EEA 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   765 RELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLsmaEAVLREHKTLVQQLKEQ--NEALNRAHV 842
Cdd:pfam09787   89 ESSREQLQELEEQLATERSARREAEAELERLQEELRYLEEELRRSKATL---QSRIKDREAEIEKLRNQltSKSQSSSSQ 165

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157738667   843 QELlqcseregalqeeradeaqqrEEELRALQEELSQAKCSSEEAQLEHAELQEQLHRANTDTAEL 908
Cdd:pfam09787  166 SEL---------------------ENRLHQLTETLIQKQTMLEALSTEKNSLVLQLERMEQQIKEL 210
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 738-1052 1.14e-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: 43.57  E-value: 1.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   738 QQQTQLIEVLTAEKGQQgvgpPTDNEARELAAQLALSQAQlEVHQGEVQRlQAQVVDLQAKM---------RAALDDQDK 808
Cdd:pfam17380  287 RQQQEKFEKMEQERLRQ----EKEEKAREVERRRKLEEAE-KARQAEMDR-QAAIYAEQERMamerereleRIRQEERKR 360

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   809 V-----QSQLSMAEAVLREHKTLVQQLKEQNE----ALNRAHVQELLQcSEREGALQEE-------RADEAQQREEELRA 872
Cdd:pfam17380  361 ElerirQEEIAMEISRMRELERLQMERQQKNErvrqELEAARKVKILE-EERQRKIQQQkvemeqiRAEQEEARQREVRR 439

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   873 LQEELSQakcSSEEAQLEHAELQEQLHRANTDTAELGIQvcALTVEKERVEEALACAVQELQDAKEAASREREGLERQVA 952
Cdd:pfam17380  440 LEEERAR---EMERVRLEEQERQQQVERLRQQEEERKRK--KLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERK 514

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   953 GLQQEKEsLQEKlkaakaaagslpglQAQLAQAEQRAQSLQEAAHQelntlkfQLSAEIMDYQSRLKNAGEECKSLRGQL 1032
Cdd:pfam17380  515 RKLLEKE-MEER--------------QKAIYEEERRREAEEERRKQ-------QEMEERRRIQEQMRKATEERSRLEAME 572

                          330       340
                   ....*....|....*....|..
gi 157738667  1033 EEQG--RQLQAAEEAVEKLKAT 1052
Cdd:pfam17380  573 REREmmRQIVESEKARAEYEAT 594
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 233-467 1.36e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 42.83  E-value: 1.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  233 DEMRLELDQLEVREKQLRERMQQLDRENQELRAAVSQQGEQLQTERERGRTAAEDNVRLTCLVAELQKQWEVTQAT-QNT 311
Cdd:COG4942    30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEElAEL 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  312 VKELQTCLQGLELGAAEKEEDYHTALRRLEsMLQPLAQELEATRDSLDKKNQHLasfpgwlamAQQKADTASDTKgrqep 391
Cdd:COG4942   110 LRALYRLGRQPPLALLLSPEDFLDAVRRLQ-YLKYLAPARREQAEELRADLAEL---------AALRAELEAERA----- 174

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157738667  392 ipsDAAQEMQELGEKLQALERERTKVEEVNRQQSAQLEQLVKELQLKEDARASLERLVKEMAPLQEELSGKGQEAD 467
Cdd:COG4942   175 ---ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 799-1118 1.39e-03

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: 43.24  E-value: 1.39e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   799 MRAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNEALNRAHVQELLQCSEREgALQEERADEAQQREEELRALQEELS 878
Cdd:pfam01576    7 MQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAE-EMRARLAARKQELEEILHELESRLE 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   879 QAKCSSEEAQLEHAELQEQL-----HRANTDTAELGIQVCALTVE---KERVEEALAcavqeLQDAKEAASREREGLERQ 950
Cdd:pfam01576   86 EEEERSQQLQNEKKKMQQHIqdleeQLDEEEAARQKLQLEKVTTEakiKKLEEDILL-----LEDQNSKLSKERKLLEER 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   951 VAGLQQEKESLQEKLKAAKAAAGSLpglQAQLAQAEQRAQSlQEAAHQELNTLKFQLSAEIMDYQSRLKNAGEECKSLRG 1030
Cdd:pfam01576  161 ISEFTSNLAEEEEKAKSLSKLKNKH---EAMISDLEERLKK-EEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRA 236

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  1031 QLEEQGRQLQAAEEAVEKLKATQADMGEKLSCTSNHLAECQ-------AAMLRKDKEGAALREDLERTQKELEK---ATT 1100
Cdd:pfam01576  237 QLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQedleserAARNKAEKQRRDLGEELEALKTELEDtldTTA 316

                          330
                   ....*....|....*...
gi 157738667  1101 KIQEYYNKLCQEVTNRER 1118
Cdd:pfam01576  317 AQQELRSKREQEVTELKK 334
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
227-752 1.64e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.13  E-value: 1.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  227 EALEGFDEMRLELDQLEVREKQLRERMQQLDRENQELRA-AVSQQGEQLQTERERGRTAA--EDNVRLTCLVAELQKQWE 303
Cdd:PRK03918  197 EKEKELEEVLREINEISSELPELREELEKLEKEVKELEElKEEIEELEKELESLEGSKRKleEKIRELEERIEELKKEIE 276

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  304 VTQATQNTVKELQ-TCLQGLELGaaEKEEDYHTALRRLESMLQPLAQELEATRDSLDKknqhlasfpgwlamAQQKADTA 382
Cdd:PRK03918  277 ELEEKVKELKELKeKAEEYIKLS--EFYEEYLDELREIEKRLSRLEEEINGIEERIKE--------------LEEKEERL 340

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  383 SDTKGRQEPIpsdaAQEMQELGEKLQALERERTKVEEVNRQQSA----QLEQLVKELQLKEDARASLERLVKEmapLQEE 458
Cdd:PRK03918  341 EELKKKLKEL----EKRLEELEERHELYEEAKAKKEELERLKKRltglTPEKLEKELEELEKAKEEIEEEISK---ITAR 413

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  459 LSGKGQEADQLWRRLQELlahtssweeELAELRREKKQQQEEKELLEQEVRSLTRQLQFLETQLAQVSQHVSDLEEQKKQ 538
Cdd:PRK03918  414 IGELKKEIKELKKAIEEL---------KKAKGKCPVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRE 484

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  539 ----------LIQDKDHLSQQVGMLERLAGPPGPELPVAGEKNEalvpvnsSLQEAWGKPEEEQRGLQEaqlDDTKVQE- 607
Cdd:PRK03918  485 lekvlkkeseLIKLKELAEQLKELEEKLKKYNLEELEKKAEEYE-------KLKEKLIKLKGEIKSLKK---ELEKLEEl 554

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  608 GSQEEELRQANRELEKELQNVVGR--------NQLLEGKLQALQADYQ---ALQQRESAIQGSLASLEAEQASIrhlgDQ 676
Cdd:PRK03918  555 KKKLAELEKKLDELEEELAELLKEleelgfesVEELEERLKELEPFYNeylELKDAEKELEREEKELKKLEEEL----DK 630

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157738667  677 MEASLLAVRKAKEAMKAQMAEKEAILQSKEGEcqQLREEVEQCQQLAEARHRELRALESQCQQQTQLIEVLTAEKG 752
Cdd:PRK03918  631 AFEELAETEKRLEELRKELEELEKKYSEEEYE--ELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELE 704
PRK09039 PRK09039
peptidoglycan -binding protein;
919-1060 1.76e-03

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 42.26  E-value: 1.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  919 KERVEEALACAVQELQDAKEAASREREGLERQVAGLQQE---KESLQEKLKaakaaaGSLPGLQAQLAQAEQRAQSLQea 995
Cdd:PRK09039   51 KDSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASlsaAEAERSRLQ------ALLAELAGAGAAAEGRAGELA-- 122

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157738667  996 ahQELNTLKfQLSAEIMdyqSRLKNAGEECKSLRGQLEEQGRQLQAAEEAVEKLKATQADMGEKL 1060
Cdd:PRK09039  123 --QELDSEK-QVSARAL---AQVELLNQQIAALRRQLAALEAALDASEKRDRESQAKIADLGRRL 181
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
959-1169 1.78e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.83  E-value: 1.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  959 ESLQEKLKAAKAAAGSLPGL---QAQLAQAEQRAQSLQEAAHQELNTLKFQLSAEIMDYQSRLKNAGEECKSLRgqleeq 1035
Cdd:COG4717    49 ERLEKEADELFKPQGRKPELnlkELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLE------ 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667 1036 grQLQAAEEAVEKLKATQADMgeklsctsNHLAECQAAMLRKDKEGAALREDLERTQKELEKATTKIQEYYNKLCQEVtn 1115
Cdd:COG4717   123 --KLLQLLPLYQELEALEAEL--------AELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLAT-- 190

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 157738667 1116 rERNDQKMLADLDDLNRTKKYLEERLIELLRDKDALWQKSDALEFQQKLSAEER 1169
Cdd:COG4717   191 -EEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEE 243
mukB PRK04863
chromosome partition protein MukB;
227-933 2.00e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 43.02  E-value: 2.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  227 EALEGFDEMRLELDQLEVREKQLRE---RMQQLDRENQELRAAVSQQGEQLQTERErgrtaaednvrltclVAELQKQWE 303
Cdd:PRK04863  500 ELLRRLREQRHLAEQLQQLRMRLSEleqRLRQQQRAERLLAEFCKRLGKNLDDEDE---------------LEQLQEELE 564

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  304 VTqatqntvkelqtcLQGLELGAAEKEEDYhTALRRLESMLQPLAQELEATRdsldkknqhlasfPGWLAmAQQKADTAS 383
Cdd:PRK04863  565 AR-------------LESLSESVSEARERR-MALRQQLEQLQARIQRLAARA-------------PAWLA-AQDALARLR 616

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  384 DTKGRQEPIPSDAAQEMQELGEKLQALERERTKVEEVNRQQSAQLEQLVKE--------LQLKEDARASL-----ERLVK 450
Cdd:PRK04863  617 EQSGEEFEDSQDVTEYMQQLLERERELTVERDELAARKQALDEEIERLSQPggsedprlNALAERFGGVLlseiyDDVSL 696

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  451 EMAPLQEELSGKGQEA------DQLWRRLQELlahtssweeelaelrrekkqqqeekelleqevRSLTRQLQFLETQLAQ 524
Cdd:PRK04863  697 EDAPYFSALYGPARHAivvpdlSDAAEQLAGL--------------------------------EDCPEDLYLIEGDPDS 744

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  525 VSQHVSDLEEQKKQLIQDkdhLSQQVGMLERLagppgPELPVAGEKN-----EALVPVNSSLQEAWGKPEEEQRGLQEAq 599
Cdd:PRK04863  745 FDDSVFSVEELEKAVVVK---IADRQWRYSRF-----PEVPLFGRAArekriEQLRAEREELAERYATLSFDVQKLQRL- 815

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  600 lddtkVQEGSQ--------------EEELRQANR---ELEKELQNVVGRNQLLEGKLQALQADYQALQQRESaiQGSLAS 662
Cdd:PRK04863  816 -----HQAFSRfigshlavafeadpEAELRQLNRrrvELERALADHESQEQQQRSQLEQAKEGLSALNRLLP--RLNLLA 888

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  663 LEAEQASIRHLGDQMEASLLAVR--KAKEAMKAQMAEKEAILQSKEGECQQLREEVEQCQQLAEARHRELRALesqcqqq 740
Cdd:PRK04863  889 DETLADRVEEIREQLDEAEEAKRfvQQHGNALAQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKQQAFAL------- 961

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  741 TQLIEVLTAEKGQQGVGPPTDNEarELAAQLalsQAQLEvhQGEVQRLQAQVVDLQAKmrAALDDQDKVQSQLSMAEAVL 820
Cdd:PRK04863  962 TEVVQRRAHFSYEDAAEMLAKNS--DLNEKL---RQRLE--QAEQERTRAREQLRQAQ--AQLAQYNQVLASLKSSYDAK 1032

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  821 REhktLVQQLKEQNEALNRAHVQELlqcseregalqEERAdeAQQREEelraLQEELS--QAKCSSEEAQL-----EHAE 893
Cdd:PRK04863 1033 RQ---MLQELKQELQDLGVPADSGA-----------EERA--RARRDE----LHARLSanRSRRNQLEKQLtfceaEMDN 1092

                         730       740       750       760
                  ....*....|....*....|....*....|....*....|..
gi 157738667  894 LQEQLHRANTDtaelgiqvcaLTVEKERVEEALA--CAVQEL 933
Cdd:PRK04863 1093 LTKKLRKLERD----------YHEMREQVVNAKAgwCAVLRL 1124
FYVE_CARP cd15750
FYVE-like domain found in caspase-associated ring proteins, CARP1 and CARP2; CARP1 and CARP2 ...
 1178-1226 2.06e-03

FYVE-like domain found in caspase-associated ring proteins, CARP1 and CARP2; CARP1 and CARP2 are a novel group of caspase regulators by the presence of a FYVE-type zinc finger domain. They do not localize to membranes in the cell and are involved in the negative regulation of apoptosis, specifically targeting two initiator caspases, caspase 8 and caspase 10, which are distinguished from other FYVE-type proteins. Moreover, these proteins have an altered sequence in the basic ligand binding patch and lack the WxxD (x for any residue) motif that is conserved only in phosphoinositide binding FYVE domains. Thus they constitute a family of unique FYVE-type domains called FYVE-like domains.


Pssm-ID: 277289 [Multi-domain]  Cd Length: 47  Bit Score: 37.34  E-value: 2.06e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 157738667 1178 HCLDCKREFSWMVRRHHCRICGRIFCYYCcnnyvLSKHGGKKeRCCRAC 1226
Cdd:cd15750     2 PCESCGAKFSVFKRKRTCADCKRYFCSNC-----LSKEERGR-RRCRRC 44
PTZ00121 PTZ00121
MAEBL; Provisional
 827-1169 2.24e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.82  E-value: 2.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  827 VQQLKEQNEALNRAHVQELLQCSEREGALQEERADEAQQREEELRALQEElsqaKCSSEEAQLEHAELQEQLHRANTDTA 906
Cdd:PTZ00121 1199 ARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEE----RNNEEIRKFEEARMAHFARRQAAIKA 1274

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  907 ELGIQVCAL--TVEKERVEEAL-ACAVQELQDAKEAA--SREREGLERQVAGLQQEKESLQEKLKAAKAAAgslpglQAQ 981
Cdd:PTZ00121 1275 EEARKADELkkAEEKKKADEAKkAEEKKKADEAKKKAeeAKKADEAKKKAEEAKKKADAAKKKAEEAKKAA------EAA 1348

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  982 LAQAEQRAQSLQEAAHQ----ELNTLKFQLSAEIMDYQSRLKNAGEECKSLRGQLEEQGRQLQAAEEAVEKL-----KAT 1052
Cdd:PTZ00121 1349 KAEAEAAADEAEAAEEKaeaaEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKAdeakkKAE 1428

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667 1053 QADMGEKLSCTSNHLAecQAAMLRKDKEGAALREDLERTQKELEKA-TTKIQEYYNKLCQEVTNRERNDQKMLADLDDLN 1131
Cdd:PTZ00121 1429 EKKKADEAKKKAEEAK--KADEAKKKAEEAKKAEEAKKKAEEAKKAdEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAA 1506

                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 157738667 1132 RTKKYLEE-RLIELLRDKDALWQKSDALEFQQKLSAEER 1169
Cdd:PTZ00121 1507 EAKKKADEaKKAEEAKKADEAKKAEEAKKADEAKKAEEK 1545
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 930-1104 2.25e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 41.45  E-value: 2.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  930 VQELQDAKEAASREREGLERQVAGLQQEKEslqeklkaakaaagslpGLQAQLAQAEQRAQSLqEAAHQELNTLKFQLSA 1009
Cdd:COG1579    12 LQELDSELDRLEHRLKELPAELAELEDELA-----------------ALEARLEAAKTELEDL-EKEIKRLELEIEEVEA 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667 1010 EIMDYQSRLKNAG--EECKSLRGQLEEQGRQLQAAE-------EAVEKLKATQADMGEKLSCTSNHLAECQAamlRKDKE 1080
Cdd:COG1579    74 RIKKYEEQLGNVRnnKEYEALQKEIESLKRRISDLEdeilelmERIEELEEELAELEAELAELEAELEEKKA---ELDEE 150

                         170       180
                  ....*....|....*....|....
gi 157738667 1081 GAALREDLERTQKELEKATTKIQE 1104
Cdd:COG1579   151 LAELEAELEELEAEREELAAKIPP 174
DUF745 pfam05335
Protein of unknown function (DUF745); This family consists of several uncharacterized ...
 797-934 2.43e-03

Protein of unknown function (DUF745); This family consists of several uncharacterized Drosophila melanogaster proteins of unknown function.


Pssm-ID: 398808 [Multi-domain]  Cd Length: 180  Bit Score: 40.63  E-value: 2.43e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   797 AKMRAALDDQDKVQSQLS--------MAEAVLREHKTLVQQL-KEQNEAlnRAHVQEL---LQCSEREGALQEERADEAQ 864
Cdd:pfam05335   23 AQAAAAEAAARQVKNQLAdkalqaakAAEAALAGKQQIVEQLeQELREA--EAVVQEEsasLQQSQANANAAQRAAQQAQ 100

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157738667   865 QREEELRAL----QEELSQAKCSSEEAQLEHAELQEQLHRANTDTAELGIQVCALTVEKERVEEAL---ACAVQELQ 934
Cdd:pfam05335  101 QQLEALTAAlkaaQANLENAEQVAAGAQQELAEKTQLLEAAKKRVERLQRQLAEARADLEKTKKAAykaACAAVEAK 177
PRK11281 PRK11281
mechanosensitive channel MscK;
516-839 3.10e-03

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 42.21  E-value: 3.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  516 QFLET---QLAQVSQHVSDLEEQKKQLIQDKDHLSQQVGMLERLAGPPGPELPVAGEK--------------------NE 572
Cdd:PRK11281   63 QDLEQtlaLLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRETLSTlslrqlesrlaqtldqlqnaQN 142

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  573 ALVPVNSSLQEAWGKPEEEQRGLQEAQ---------LDDTKVQEGSQEEELRQanrELEKELQNVVGRN----QLLEG-- 637
Cdd:PRK11281  143 DLAEYNSQLVSLQTQPERAQAALYANSqrlqqirnlLKGGKVGGKALRPSQRV---LLQAEQALLNAQNdlqrKSLEGnt 219

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  638 KLQAL---QADYQALQQresaiqgslASLEAEQASIRHLGDQ--MEASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQL 712
Cdd:PRK11281  220 QLQDLlqkQRDYLTARI---------QRLEHQLQLLQEAINSkrLTLSEKTVQEAQSQDEAARIQANPLVAQELEINLQL 290

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  713 REE-VEQCQQLAEARHRELRA---LESQCQQQTQLIEVLTAEKG---------QQGVGPPTDNEARELAAQLA-LSQAQL 778
Cdd:PRK11281  291 SQRlLKATEKLNTLTQQNLRVknwLDRLTQSERNIKEQISVLKGslllsrilyQQQQALPSADLIEGLADRIAdLRLEQF 370

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157738667  779 EVHQ--GEVQRLQAQVVDLQAKMRAALDDQdkvqsqlsmaeavlrEHKTLVQQLKEQNEALNR 839
Cdd:PRK11281  371 EINQqrDALFQPDAYIDKLEAGHKSEVTDE---------------VRDALLQLLDERRELLDQ 418
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
510-745 3.18e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 41.93  E-value: 3.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  510 SLTRQLQFLETQLAQVSQHVSDLEEQKKQLIQDKD--HLSQQVGMLErlagppgpelpvageknEALVPVNSSLQEAwgk 587
Cdd:COG3206   172 EARKALEFLEEQLPELRKELEEAEAALEEFRQKNGlvDLSEEAKLLL-----------------QQLSELESQLAEA--- 231

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  588 peEEQRGLQEAQLDDTKVQEGSQEEELRQANREleKELQNVVGRNQLLEGKLQALQADYQ----ALQQRESAIQGSLASL 663
Cdd:COG3206   232 --RAELAEAEARLAALRAQLGSGPDALPELLQS--PVIQQLRAQLAELEAELAELSARYTpnhpDVIALRAQIAALRAQL 307

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  664 EAEQASIRHLGDQMEASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEVEQCQQLAE---ARHRELRALESQCQQQ 740
Cdd:COG3206   308 QQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYEsllQRLEEARLAEALTVGN 387


                  ....*
gi 157738667  741 TQLIE 745
Cdd:COG3206   388 VRVID 392
PRK11281 PRK11281
mechanosensitive channel MscK;
978-1164 3.70e-03

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 41.82  E-value: 3.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  978 LQAQLAQAEQRAQ--SLQEAAHQELNTLKFQLsAEIMDYQSRLKnageeckSLRGQLEEQGRQLQAAEEAVEKLKATQAD 1055
Cdd:PRK11281   41 VQAQLDALNKQKLleAEDKLVQQDLEQTLALL-DKIDRQKEETE-------QLKQQLAQAPAKLRQAQAELEALKDDNDE 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667 1056 MGE-------------KLSCTSNHLAECQAAMLRKDKEGAALREDLERTQKELEKATTKIQEYYNKLCQEVTNRE--RND 1120
Cdd:PRK11281  113 ETRetlstlslrqlesRLAQTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANSQRLQQIRNLLKGGKVGGKalRPS 192

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 157738667 1121 QKM-----LADLD---DLNRTKKYLEERLIELLRDK-DALWQKSDALEFQQKL 1164
Cdd:PRK11281  193 QRVllqaeQALLNaqnDLQRKSLEGNTQLQDLLQKQrDYLTARIQRLEHQLQL 245
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 590-1050 3.84e-03

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


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 41.65  E-value: 3.84e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   590 EEQRGLQEAQLDDTKVQEGSQEEELRQANRELEKELQNVVGRNQLLEGKLQALQADYQALQQRESAIQGSLASLEAEQAS 669
Cdd:pfam05557   92 LNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQR 171

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   670 IRHLGD--QMEASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEVEQCQQLAEARHRELRALESQCQQQTQLIEV- 746
Cdd:pfam05557  172 IKELEFeiQSQEQDSEIVKNSKSELARIPELEKELERLREHNKHLNENIENKLLLKEEVEDLKRKLEREEKYREEAATLe 251

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   747 LTAEKGQQ------------GVGPPTDNEARELAAQLalsQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLS 814
Cdd:pfam05557  252 LEKEKLEQelqswvklaqdtGLNLRSPEDLSRRIEQL---QQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIE 328

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   815 MAEAVLREHKTLVQQLKEQNEALN--RAHVQELLQCSEREGALQEERADEAQQREEELRALQEelSQAKCSSEEAQLEHA 892
Cdd:pfam05557  329 DLNKKLKRHKALVRRLQRRVLLLTkeRDGYRAILESYDKELTMSNYSPQLLERIEEAEDMTQK--MQAHNEEMEAQLSVA 406

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   893 ELQEQLHRANTDTAELGIQVCAltvEKERVEEALACA--VQELQDAKEAASREREGLERQVAGLQQEKESLQEKLKAAKA 970
Cdd:pfam05557  407 EEELGGYKQQAQTLERELQALR---QQESLADPSYSKeeVDSLRRKLETLELERQRLREQKNELEMELERRCLQGDYDPK 483

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667   971 AAGSLPGLQAQLAQAEQRAQSLQEAAHQELNTLKFQLSAEIMDYQSRLKNAGEECKSLRGQLEEQGRQLQAAEEAVEKLK 1050
Cdd:pfam05557  484 KTKVLHLSMNPAAEAYQQRKNQLEKLQAEIERLKRLLKKLEDDLEQVLRLPETTSTMNFKEVLDLRKELESAELKNQRLK 563
FYVE_WDFY1 cd15756
FYVE domain found in WD40 repeat and FYVE domain-containing protein 1 (WDFY1) and similar ...
 1169-1232 4.46e-03

FYVE domain found in WD40 repeat and FYVE domain-containing protein 1 (WDFY1) and similar proteins; WDFY1, also termed FYVE domain containing protein localized to endosomes-1 (FENS-1), or phosphoinositide-binding protein 1, or zinc finger FYVE domain-containing protein 17, is a novel single FYVE domain containing protein that binds phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) with high specificity over other phosphoinositides. WDFY1 to early endosomes requires an intact FYVE domain and is inhibited by wortmannin, a PI3-kinase inhibitor. In addition to FYVE domain, WDFY1 harbors multiple WD-40 repeats.


Pssm-ID: 277295 [Multi-domain]  Cd Length: 76  Bit Score: 37.36  E-value: 4.46e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157738667 1169 RWLgdtEANHCLDCKREFSWMV-----------RRHHCRICGRIFCYYCCNNYVLSKHGG--KKERCCRACFQKLSE 1232
Cdd:cd15756     2 QWL---ESDSCQKCEQPFFWNIkqmwdtktlglRQHHCRKCGQAVCGKCSSKRSSYPIMGfeFQVRVCDSCFETIKD 75
PRK11281 PRK11281
mechanosensitive channel MscK;
796-1061 4.81e-03

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 41.44  E-value: 4.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  796 QAKMRAALDDQDKVQSQLsmaeAVLREHKTLVQQLKEQNEALNRAhvQELLQCSERegalQEERADEAQQR----EEELR 871
Cdd:PRK11281   28 RAASNGDLPTEADVQAQL----DALNKQKLLEAEDKLVQQDLEQT--LALLDKIDR----QKEETEQLKQQlaqaPAKLR 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  872 ALQEELSQAKCSSEE-----------AQLEH--AELQEQLHRANTDTAELGIQVCALTVEKERVEEALACAVQELQDake 938
Cdd:PRK11281   98 QAQAELEALKDDNDEetretlstlslRQLESrlAQTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANSQRLQQ--- 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  939 aasreregLERQVAGLQQEKE----SLQEKLKAAKAAAGSLPGLQAQLAQAEQRAQSLQEAAHQELNTLKFQLSAEIMDY 1014
Cdd:PRK11281  175 --------IRNLLKGGKVGGKalrpSQRVLLQAEQALLNAQNDLQRKSLEGNTQLQDLLQKQRDYLTARIQRLEHQLQLL 246

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 157738667 1015 QS-----RLKnageeckslrgQLEEQGRQLQAAEEAVE----KLKATQADMGEKLS 1061
Cdd:PRK11281  247 QEainskRLT-----------LSEKTVQEAQSQDEAARiqanPLVAQELEINLQLS 291
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
729-843 5.50e-03

Multidrug resistance efflux pump EmrA [Defense mechanisms];


Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 40.80  E-value: 5.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  729 ELRALESQCQQQTQLIEVLTAEKGQQgvgpptdNEARELAAQLALSQAQLEVHQGEVQRL----------QAQVVDLQAK 798
Cdd:COG1566    84 ALAQAEAQLAAAEAQLARLEAELGAE-------AEIAAAEAQLAAAQAQLDLAQRELERYqalykkgavsQQELDEARAA 156

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 157738667  799 MRAALDDQDKVQSQLSMAEAVLREHKTLVQ---QLKEQNEALNRAHVQ 843
Cdd:COG1566   157 LDAAQAQLEAAQAQLAQAQAGLREEEELAAaqaQVAQAEAALAQAELN 204
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 583-725 5.90e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 40.95  E-value: 5.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  583 EAWGKPEEEQRGLQEAQLDDTKVQEGSQEEELRQANRELEKELQNVVGRNQLLEGKLQALQADYQALQQRESAIQGslAS 662
Cdd:PRK09510   62 EQYNRQQQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEA--AA 139

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157738667  663 LEAEQASIRHLGDQMEASLLAVRKAKEAMK---AQMAEKEAILQSKEGECQQLREEVEQCQQLAEA 725
Cdd:PRK09510  140 KAAAAAKAKAEAEAKRAAAAAKKAAAEAKKkaeAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEA 205
PRK09039 PRK09039
peptidoglycan -binding protein;
761-934 6.72e-03

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 40.33  E-value: 6.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  761 DNEARELAAQLA-LSQAqLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAvlrehktlvqqlkeqneALNR 839
Cdd:PRK09039   52 DSALDRLNSQIAeLADL-LSLERQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAG-----------------AGAA 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  840 AhvqellqcSEREGALQEERADEAQQREEELRalQEELSQAKCSSEEAQLehAELQEQLHRANTDTAELGIQVCALtveK 919
Cdd:PRK09039  114 A--------EGRAGELAQELDSEKQVSARALA--QVELLNQQIAALRRQL--AALEAALDASEKRDRESQAKIADL---G 178

                         170
                  ....*....|....*
gi 157738667  920 ERVEEALACAVQELQ 934
Cdd:PRK09039  179 RRLNVALAQRVQELN 193
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 702-881 7.18e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 39.91  E-value: 7.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  702 LQSKEGECQQLREEVEQCQQLAEARHRELRALESQCQQQTQLIEVLTAEKGQQgvgpptDNEARELAAQLALSQAQLEVH 781
Cdd:COG1579    12 LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRL------ELEIEEVEARIKKYEEQLGNV 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  782 QG--EVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNEALNRAHVQELLQCSEREGALQEER 859
Cdd:COG1579    86 RNnkEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAER 165

                         170       180
                  ....*....|....*....|..
gi 157738667  860 ADEAQQREEELRALQEELSQAK 881
Cdd:COG1579   166 EELAAKIPPELLALYERIRKRK 187
PRK10929 PRK10929
putative mechanosensitive channel protein; Provisional
 789-1006 7.87e-03

putative mechanosensitive channel protein; Provisional


Pssm-ID: 236798 [Multi-domain]  Cd Length: 1109  Bit Score: 40.81  E-value: 7.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  789 QAQVVD-LQAKMRAaLDDQDKVQSQLSMAEAVLREHKTLVQQLKEQ--NEALNRAHV----------QELLQCSERegaL 855
Cdd:PRK10929   43 QAEIVEaLQSALNW-LEERKGSLERAKQYQQVIDNFPKLSAELRQQlnNERDEPRSVppnmstdaleQEILQVSSQ---L 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  856 QEErADEAQQREEELRALQEELSQAKCSSEEAQLEHAELQEQLHRANTDTAELG-IQVCALTVE----KERVEEaLACAV 930
Cdd:PRK10929  119 LEK-SRQAQQEQDRAREISDSLSQLPQQQTEARRQLNEIERRLQTLGTPNTPLAqAQLTALQAEsaalKALVDE-LELAQ 196

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  931 ------QELQDAK-EAASREREGLERQVAGL--------QQEKESLQEKLKAAKAAAGSLP-GLQAQLAQAEQRAQSLQE 994
Cdd:PRK10929  197 lsannrQELARLRsELAKKRSQQLDAYLQALrnqlnsqrQREAERALESTELLAEQSGDLPkSIVAQFKINRELSQALNQ 276

                         250
                  ....*....|..
gi 157738667  995 AAhQELNTLKFQ 1006
Cdd:PRK10929  277 QA-QRMDLIASQ 287
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 372-631 8.08e-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: 8.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  372 LAMAQQKADTASDTKGRQEpipsDAAQEMQELGEKLQALERERTKVEEVNRQQSAQLEQLVKELQLKED----ARASLER 447
Cdd:COG4942    12 ALAAAAQADAAAEAEAELE----QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQelaaLEAELAE 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  448 LVKEMAPLQEELSgkgQEADQLWRRLQELLAHTSSWEEELAELRREKKQQQEEKELLEQEVRSLTRQLQFLETQLAQVSQ 527
Cdd:COG4942    88 LEKEIAELRAELE---AQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAA 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  528 HVSDLEEQKKQLIQDKDHLSQQVGMLERLagppgpelpvAGEKNEALVPVNSSLQEAwgkpEEEQRGLQEAQLDDTKVQE 607
Cdd:COG4942   165 LRAELEAERAELEALLAELEEERAALEAL----------KAERQKLLARLEKELAEL----AAELAELQQEAEELEALIA 230

                         250       260
                  ....*....|....*....|....
gi 157738667  608 GSQEEELRQANRELEKELQNVVGR 631
Cdd:COG4942   231 RLEAEAAAAAERTPAAGFAALKGK 254
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 519-736 9.06e-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: 9.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  519 ETQLAQVSQHVSDLEEQKKQLIQDKDHLSQQVGmlerlagppgpelpvagEKNEALVPVNSSLQEAwgkpeEEQRGLQEA 598
Cdd:COG3883    15 DPQIQAKQKELSELQAELEAAQAELDALQAELE-----------------ELNEEYNELQAELEAL-----QAEIDKLQA 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  599 QLDDTKVQEGSQEEELRQANRELEKELQNVVGRNQLLEGK--------LQALQADYQALQQRESAIQGSLASLEAEQASI 670
Cdd:COG3883    73 EIAEAEAEIEERREELGERARALYRSGGSVSYLDVLLGSEsfsdfldrLSALSKIADADADLLEELKADKAELEAKKAEL 152

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157738667  671 RHLGDQMEASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEVEQCQQLAEARHRELRALESQ 736
Cdd:COG3883   153 EAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
240-478 9.52e-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: 9.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  240 DQLEVREKQLRERMQQLDRENQELRAAVSQQGEQLQTERERGRTAAEDnvrltclvaelqkqwEVTQATQNTVKELQTCL 319
Cdd:COG3206   164 QNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLS---------------EEAKLLLQQLSELESQL 228

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  320 QGLELGAAEKEEDYHTALRRLESMLQPLAQELEatrdsldkkNQHLASFPGWLAMAQQKADTASDTKGRQEPipsdaaqE 399
Cdd:COG3206   229 AEARAELAEAEARLAALRAQLGSGPDALPELLQ---------SPVIQQLRAQLAELEAELAELSARYTPNHP-------D 292

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  400 MQELGEKLQALERE-RTKVEEVNRQQSAQLEQLVKELQLKEDARASLERLVKEMAPLQEELSGKGQEADQLWRRLQELLA 478
Cdd:COG3206   293 VIALRAQIAALRAQlQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQ 372
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
 224-478 9.73e-03

Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444066 [Multi-domain]  Cd Length: 594  Bit Score: 40.33  E-value: 9.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  224 LNNEALEGFDEMRLELDQLEVREKQLRERMQQLDRENQELRAAVSQQGEQLQTERErgrtaaednvrltclvAELQKQWE 303
Cdd:COG5185   280 LNENANNLIKQFENTKEKIAEYTKSIDIKKATESLEEQLAAAEAEQELEESKRETE----------------TGIQNLTA 343

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  304 VTQATQNTVKELQTclqglELGAAEKEEDYHTALRRLESMLQPLAQELEATRDSLDKKNQHlasfpgWLAMAQQKADTAS 383
Cdd:COG5185   344 EIEQGQESLTENLE-----AIKEEIENIVGEVELSKSSEELDSFKDTIESTKESLDEIPQN------QRGYAQEILATLE 412

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738667  384 DTKGRQEpipsdaaQEMQELGEKLQALERERTKVEEVNRQQSAQLEQLVKELQLKEDARASlERLVKEMAPLQEELSGKG 463
Cdd:COG5185   413 DTLKAAD-------RQIEELQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQSRLE-EAYDEINRSVRSKKEDLN 484

                         250
                  ....*....|....*
gi 157738667  464 QEADQLWRRLQELLA 478
Cdd:COG5185   485 EELTQIESRVSTLKA 499
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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