|
Name |
Accession |
Description |
Interval |
E-value |
| RUN_RUFY3 |
cd17696 |
RUN domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar proteins; ... |
128-283 |
9.86e-101 |
|
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: 301.92 E-value: 9.86e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 128 ERMNLMNMAKLSIKGLIESALNLGRTLDSDYAPLQQFFVVMEHCLKHGLKAKKTFLGQNKSFWGPLELVEKLVPEAAEIT 207
Cdd:cd17696 1 ERMNLMNMAKLSIKGLIESALNLGRTLDSDYAPLQQFFVVMEHCLKHGLKAKKTFLGQNKSFWGPLELVEKLVPEAAEIT 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767931431 208 ASVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINKKELLSEFYEPNALMMEEEGAIIAGLLVGLNVIDANFC 283
Cdd:cd17696 81 ASVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINRKDLLSEFYEPNALMMEEEGAIIAGLLVGLNVIDANFC 156
|
|
| RUN_RUFY2 |
cd17695 |
RUN domain found in RUN and FYVE domain-containing protein 2 (RUFY2) and similar proteins; ... |
128-283 |
1.45e-97 |
|
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: 293.81 E-value: 1.45e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 128 ERMNLMNMAKLSIKGLIESALNLGRTLDSDYAPLQQFFVVMEHCLKHGLKAKKTFLGQNKSFWGPLELVEKLVPEAAEIT 207
Cdd:cd17695 1 ERANLLNMAKLSIKGLIESALSFGRTLDSDYPPLQQFFVVMEHCLKHGLKVRKSFLSYNKTIWGPLELVEKLCPEAEEIA 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767931431 208 ASVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINKKELLSEFYEPNALMMEEEGAIIAGLLVGLNVIDANFC 283
Cdd:cd17695 81 ASVRDLPGLKTPLGRARAWLRLALMQKKLADYLRCLIIRRDLLSEFYEYHALMMEEEGAVIVGLLVGLNVIDANLC 156
|
|
| RUN_RUFY1_like |
cd17681 |
RUN domain found in RUN and FYVE domain-containing proteins, RUFY1, RUFY2, RUFY3 and similar ... |
128-282 |
1.76e-96 |
|
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: 291.01 E-value: 1.76e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 128 ERMNLMNMAKLSIKGLIESALNLGRTLDSDYAPLQQFFVVMEHCLKHGLKAKKTFLGQNKSFWGPLELVEKLVPEAAEIT 207
Cdd:cd17681 1 ERRNLLNLAKLSIKELIESALSFGRTLDSDHVPLQQFFVILEHVLRHGLKVKKSFLGPNKSFWPVLEHVEKLVPEANEIT 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767931431 208 ASVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINKKELLSEFYEPNALMMEEEGAIIAGLLVGLNVIDANF 282
Cdd:cd17681 81 ASVRDLPGIKTPLGRARAWLRLALMQKKLADYFRALIENKDLLSEFYEPGALMMSEEAVVIAGLLVGLNVIDCNL 155
|
|
| RUN_RUFY1 |
cd17694 |
RUN domain found in RUN and FYVE domain-containing protein 1 (RUFY1) and similar proteins; ... |
128-283 |
6.71e-93 |
|
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: 281.79 E-value: 6.71e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 128 ERMNLMNMAKLSIKGLIESALNLGRTLDSDYAPLQQFFVVMEHCLKHGLKAKKTFLGQNKSFWGPLELVEKLVPEAAEIT 207
Cdd:cd17694 1 ERANLMNMMKLSIKVLIQSALSLGRTLDSDYPPLQQFFVVLEHCLKHGLKVKKSFIGQNKSFFGPLELVEKLCPEASDIA 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767931431 208 ASVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINKKELLSEFYEPNALMMEEEGAIIAGLLVGLNVIDANFC 283
Cdd:cd17694 81 TSARNLPELKTAVGRGRAWLHLALMQKKLADYLKVLIDRKDLLSEFYEPGALMMEEEGAVIVGLLVGLNVIDANLC 156
|
|
| RUN |
pfam02759 |
RUN domain; This domain is present in several proteins that are linked to the functions of ... |
163-286 |
1.20e-45 |
|
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: 157.44 E-value: 1.20e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 163 QFFVVMEHCLKHGLKA------KKTFLGQNKSFWGPLELVEKLVPEAAEITASVKDLPGLKT---PVGRGRAWLRLALMQ 233
Cdd:pfam02759 1 QLCAALEALLSHGLKRssllilRAAGLLPERSFWALLERVGKLVPPAEELLSSVQELEQIHTpysPDGRGRAWIRLALNE 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 767931431 234 KKLSEYMKALINKKELLSEFYEPNALMMEEEGA-IIAGLLVGLNVIDANFCMKG 286
Cdd:pfam02759 81 KLLDQWLKLLLSNKELLSEYYEPWALLADPEFGeILLGLLVGLSALDFNLCLKL 134
|
|
| RUN_RUNDC3 |
cd17684 |
RUN domain found in RUN domain-containing protein 3 (RUNDC3) and similar proteins; RUNDC3 ... |
131-282 |
8.86e-37 |
|
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: 134.06 E-value: 8.86e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 131 NLMNMAKLSIKGLIESALNlgRTLDSDYAPLQQFFVVMEHCLKHGLKAKKTFLG--QNKSFWGPLELVEKLVPEAAeiTA 208
Cdd:cd17684 1 NLVTVCRLSVKSLIDKACL--ETIDDSSEELINFAAILEQILSHRLKPVKPWYGseEPRTFWDYIRVACKKVPQNC--IA 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767931431 209 SVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINKKELLSEFYEPNALMMEEEGAIIAGLLVGLNVIDANF 282
Cdd:cd17684 77 SIEQMENIKSPKAKGRAWIRVALMEKRLSEYLSTALKQTRLTRNFYQDGAIMLSEDATVLCGMLIGLNAIDFSF 150
|
|
| RUN |
cd17671 |
RUN domain; RUN domain, named after RPIP8 (Rap2 interacting protein 8), UNC-14 and NESCA (new ... |
139-282 |
7.66e-34 |
|
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: 126.00 E-value: 7.66e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 139 SIKGLIESALNLGR-------TLDSDYAPLQQFFVVMEHCLKHGLKAKKtFLGQNKSFWGPLELVEKLVPEAAEITA--S 209
Cdd:cd17671 2 AVKELLESFADNGEaddsaalTLTDDDPVVGRLCAALEAILSHGLKPKR-FGGGKVSFWDFLEALEKLLPAPSLKQAirD 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767931431 210 VKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINKKELLSEFYEPNALMM-EEEGAIIAGLLVGLNVIDANF 282
Cdd:cd17671 81 INSLSNVKTDDGRGRAWIRLALNEKSLESYLAALLSDQSLLRKYYEPWALLRdPEEAELFLSLLVGLSSLDFNL 154
|
|
| RUN_RUNDC3B |
cd17700 |
RUN domain found in RUN domain-containing protein 3B (RUNDC3B) and similar proteins; RUN ... |
131-283 |
1.63e-26 |
|
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: 105.44 E-value: 1.63e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 131 NLMNMAKLSIKGLIESALNlgRTLDSDYAPLQQFFVVMEHCLKHGLKAKKTFLGQN--KSFWGPLELVEKLVPEAAeiTA 208
Cdd:cd17700 1 NLITVCRFSVKTLIDRSCF--ETIDDSSPEFVNFAAILEQILSHRLKGQVTWFGYEspRSFWDYIRVACSKVPHNC--IC 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767931431 209 SVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINKKELLSEFYEPNALMMEEEGAIIAGLLVGLNVIDANFC 283
Cdd:cd17700 77 SIENMENVSSSRAKGRAWIRVALMEKRLSEYISTALRDFKTTRRFYEDGAIVLGEEANMLAGMLLGLNAIDFSFC 151
|
|
| RUN_RUNDC3A |
cd17699 |
RUN domain found in RUN domain-containing protein 3A (RUNDC3A) and similar proteins; RUN ... |
131-283 |
6.59e-24 |
|
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: 98.17 E-value: 6.59e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 131 NLMNMAKLSIKGLIESALnlGRTLDSDYAPLQQFFVVMEHCLKHGLKAKKTFL---GQnKSFWGPLELVEKLVPEaaEIT 207
Cdd:cd17699 1 NLITVCRFSVKTLLEKYT--AEPIDDSSEEFVNFAAILEQILSHRFKGPVSWFssdGQ-RGFWDYIRLACSKVPN--NCI 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767931431 208 ASVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINKKELLSEFYEPNALMMEEEGAIIAGLLVGLNVIDANFC 283
Cdd:cd17699 76 SSIENMENISTSRAKGRAWIRVALMEKRLSEYIATALRDTRTTRRFYDDGAIMLREESTVLTGMLIGLSAIDFSFC 151
|
|
| RUN |
smart00593 |
domain involved in Ras-like GTPase signaling; |
223-285 |
2.83e-19 |
|
domain involved in Ras-like GTPase signaling;
Pssm-ID: 214736 [Multi-domain] Cd Length: 64 Bit Score: 81.89 E-value: 2.83e-19
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767931431 223 GRAWLRLALMQKKLSEYMKALINKKELLSEFYEPNALMM-EEEGAIIAGLLVGLNVIDANFCMK 285
Cdd:smart00593 1 FRAWIRLALNEKLLSSWLNLLLSDEELLSKYYEPWAFLRdPEEGEQLLGLLVGLSALDFNLPVD 64
|
|
| RUN_RUFY4_like |
cd17682 |
RUN domain found in RUN and FYVE domain-containing protein 4 (RUFY4), FYVE and coiled-coil ... |
140-279 |
2.00e-17 |
|
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: 79.58 E-value: 2.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 140 IKGLIESALNLGRTLDSDYAP-LQQFFVVMEHCLKHGLKAKKTFLGQNKSFWGPLE-LVEKLVPEA---AEITASVKDLP 214
Cdd:cd17682 2 LKGCVLDLKSEFGEITDPDNPyLRPFCETLEKILRKGLKEKVSLGGRRKDYWDWLEeLLKKLNKIPkslSDAVKFVKSCK 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767931431 215 GLKTPVGRGRAWLRLALMQKKLSEYMKALINKKELLSEFYEPNALMMEEE-GAIIAGLLVGLNVID 279
Cdd:cd17682 82 KVKTNQGRGRLFIRYALNKKCLHDPVQQLVKNPKLLSDYYSPDSILGNEIlSEILLSLLYQLNEIN 147
|
|
| RUN_PLEKHM1 |
cd17679 |
RUN domain found in pleckstrin homology domain-containing family M member 1 (PLEKHM1) and ... |
129-275 |
2.96e-14 |
|
RUN domain found in pleckstrin homology domain-containing family M member 1 (PLEKHM1) and similar proteins; PLEKHM1, also called PH domain-containing family M member 1, or 162 kDa adapter protein (AP162), may act as a multivalent adapter protein that regulates Rab7-dependent and HOPS complex-dependent fusion events in the endolysosomal system and couples autophagic and the endocytic trafficking pathways. This model represents the RUN domain of PLEKHM1.
Pssm-ID: 439041 [Multi-domain] Cd Length: 171 Bit Score: 71.08 E-value: 2.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 129 RMNLMNMAKLSIKGLIESALNLGRTLDSDYAPLQQFFVVMEHCLKHGLKAK-----KTFLGQN------KSFWGPLELV- 196
Cdd:cd17679 1 KKSLTKELSSSVKELQLEYVSSDEVVTSSDDGANTLCCVLEAIFLHGLKDKfiskvSSVFSGDvdklpePNFWPLLLKFs 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 197 EKlvpeaaEITASVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINKKELLSEFYEPNALMM-EEEGAIIAGLLVGL 275
Cdd:cd17679 81 HR------DVIDQIEHLSQITTDVGRCRAWIRLALNDGLLESYLEAILKDKSALKSYYNPSAFLRdPEQLDILKSLLQGL 154
|
|
| RUN_SNX29 |
cd17689 |
RUN domain found in sorting nexin-29 (SNX29) and similar proteins; SNX29, also called RUN ... |
213-278 |
9.03e-13 |
|
RUN domain found in sorting nexin-29 (SNX29) and similar proteins; SNX29, also called RUN domain-containing protein 2A (RUNDC2A), belongs to the sorting nexin family. Sorting nexins are a large group of proteins that are localized in the cytoplasm and have the potential for membrane association either through their lipid-binding PX domain, a phospholipid-binding motif, or through protein-protein interactions with membrane-associated protein complexes. Some sorting nexin family members have been shown to facilitate protein sorting. This model contains the RUN domain of SNX29.
Pssm-ID: 439051 Cd Length: 166 Bit Score: 66.49 E-value: 9.03e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767931431 213 LPGLKTPVGRGRAWLRLALMQKKLSEYMKALINKKELLSEFYEPNALMM-EEEGAIIAGLLVGLNVI 278
Cdd:cd17689 93 LKNIWTDIGRGRAWLRSALNEHSLERYLHILLSNENLLRQYYEDWAFLRdEERSSMLPNMAAGLGSI 159
|
|
| RUN_RUFY4 |
cd17697 |
RUN domain found in RUN and FYVE domain-containing protein 4 (RUFY4) and similar proteins; ... |
168-278 |
8.39e-12 |
|
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: 63.28 E-value: 8.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 168 MEHCLKHGLKAKKTFLGQNKSFWGPLELVEKLVPEAAEITASVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINKK 247
Cdd:cd17697 35 LEYLLQFDQKEKKSFFGSRKDYWDFLCLCLNRHRGGTEGIHFVNSTDKLKTPLGKGRAFIRYCLVQQQLAESLQLCLLNP 114
|
90 100 110
....*....|....*....|....*....|..
gi 767931431 248 ELLSEFYEPNA-LMMEEEGAIIAGLLVGLNVI 278
Cdd:cd17697 115 ELTGEWYYARSpFLSPELRSDILDSLYELNGV 146
|
|
| RUN_SGSM1_like |
cd17687 |
RUN domain found in small G protein signaling modulators, SGSM1, SGSM2, and similar proteins; ... |
169-279 |
5.34e-11 |
|
RUN domain found in small G protein signaling modulators, SGSM1, SGSM2, and similar proteins; SGSM1, also called RUN and TBC1 domain-containing protein 2 (RUTBC2), interacts with numerous Rab family members, functioning as Rab effector for some, and as GTPase activator for others. It is a Rab9A effector and GTPase-activating protein for Rab36, and links Rab9A function to Rab36 function in the endosomal system. SGSM2, also called RUN and TBC1 domain-containing protein 1 (RUTBC1), is a GTPase-activating protein for Rab32/38, and regulates melanogenic enzyme trafficking in melanocytes. It also acts as a Rab9A effector that activates GTP hydrolysis by Rab32 and Rab33B proteins. This model contains the RUN domain of SGSM1 and SGSM2.
Pssm-ID: 439049 Cd Length: 161 Bit Score: 61.15 E-value: 5.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 169 EHCLKHGLKAKK-TFLGQNKSFwGPLELVEKLVPEAAEITASVKDL------PGLKTPVGRGRA-------------WLR 228
Cdd:cd17687 31 DACLLHGLRKRAlGLFRSSSTF-SLLQKVAKSCPPAADILRKVQEIenlsenKRSSSSSGSNSSnshgnsssnrkilWIR 109
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 767931431 229 LALMQKKLSEYMKALINKKellSEFYEPNALMME-EEGAIIAGLLVGLNVID 279
Cdd:cd17687 110 IALFEKVLDKIVDYLVENA---SKYYEKEALMADpVDGPLLASLLVGPCALD 158
|
|
| RUN_PLEKHM2 |
cd17680 |
RUN domain found in pleckstrin homology domain-containing family M member 2 (PLEKHM2) and ... |
139-260 |
5.66e-11 |
|
RUN domain found in pleckstrin homology domain-containing family M member 2 (PLEKHM2) and similar proteins; PLEKHM2, also called PH domain-containing family M member 2, or Salmonella-induced filaments A (SifA) and Kinesin-Interacting Protein (SKIP), is the lysosome, melanosome and lytic granule cargo adaptor that controls lysosome positioning using a composite kinesin-1 heavy and light chain-binding domain. In addition to kinesin-1, it also interacts with several Rabs to affect endosomal trafficking. This model represents the RUN domain of PLEKHM2.
Pssm-ID: 439042 Cd Length: 145 Bit Score: 60.72 E-value: 5.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 139 SIKGLIESALNLGRTLDSDYAPLQQFFVVMEHCLKHGLKAKktflgqNKSFWGpleLVEKLVPEAAEItaSVKDLPGLKT 218
Cdd:cd17680 12 SLQSYSSSQEEEDVLITNENRELQRLCEALDHALLHGLRRG------NRGYWP---FVKEFTHKETIK--QIENLPNVTT 80
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 767931431 219 PVGRGRAWLRLALMQKKLSEYMKALINKKELLSEFYEPNALM 260
Cdd:cd17680 81 DLGRGRAWLYLALNEGSLESYLRSFLENRKLVKKFYHKHALL 122
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
316-567 |
1.55e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.19 E-value: 1.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 316 QITAILDQKNYVEELNRHLNATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESSyILESNRKGPKQDR 395
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELA-RLEQDIARLEERR 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 396 TAEGQALSEARKHLKEETQLRLDVEKELEMQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKLQSS 475
Cdd:COG1196 312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 476 DlgvKQKSELNSRLEEKTNQMAAtIKQLEQRLRQAERSRQSAELDNRLFKQDFGDKINSLQLEVEELTRQRNQLELELKQ 555
Cdd:COG1196 392 L---RAAAELAAQLEELEEAEEA-LLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAE 467
|
250
....*....|..
gi 767931431 556 EKERRLQNDRSI 567
Cdd:COG1196 468 LLEEAALLEAAL 479
|
|
| RUN_FYCO1 |
cd17698 |
RUN domain found in FYVE and coiled-coil domain-containing protein 1 (FYCO1) and similar ... |
134-282 |
2.44e-10 |
|
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: 59.32 E-value: 2.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 134 NMAKLSIKGLIESALNLGRTLDSDYAP-------LQQFFVVMEHCLKHGLKAKKTFLGQNKSFWGPL-ELVEKlVPEAAE 205
Cdd:cd17698 2 SQLQKIIRDLQDCVTELKKEFEETGEPitddsttLHKFCAKLEYLLQFDQKEKTTLLGGRKDYWDYFcECLAK-VKGLND 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767931431 206 ITASVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINKKELLSEFYEP-NALMMEEEGAIIAGLLVGLNviDANF 282
Cdd:cd17698 81 GIRFVKSLKEVRTSLGKGRAFIRYSLVHQRLADTLQQCVMNGKVTSDWYYPrSVFLNHKYSSDIINSLYDLN--EVQF 156
|
|
| RUN1_DENND5 |
cd17677 |
RUN1 domain found in DENN domain-containing protein 5 (DENND5) and similar proteins; DENND5 ... |
174-283 |
5.87e-10 |
|
RUN1 domain found in DENN domain-containing protein 5 (DENND5) and similar proteins; DENND5 has been characterized as Rab6-interacting protein which is composed of an N-terminal DENN (Differentially Expressed in Normal and Neoplastic cells) domain followed by two RUN (RPIP8 [RaP2-interacting protein 8], UNC-14, and NESCA [new molecule containing SH3 at the carboxyl terminus]) domains flanking a PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain. It functions in membrane trafficking at a crossroads between the Golgi and the endosomal system. DENND5 has two isoforms, DENND5A and DENND5B. This model represents the first RUN domain of DENND5.
Pssm-ID: 439039 Cd Length: 183 Bit Score: 58.95 E-value: 5.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 174 HGLKAKktflgQNKS-FWGPL----ELVEKLVPEAAEITA---SVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALIN 245
Cdd:cd17677 65 HGLQTK-----QGKSaLWSHLlayqENEERLKPLPESLLFdmkNVQNMKEIKTDVGYARAWIRLALEKKLLSKHLKTLLS 139
|
90 100 110
....*....|....*....|....*....|....*....
gi 767931431 246 KKELLSEFYEPNA-LMMEEEGAIIAGLLVGLNVIDAnFC 283
Cdd:cd17677 140 NQDLLRSLYKRYAfLRCEDEREQFLYHLLSLNAVDY-FC 177
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
314-565 |
6.62e-10 |
|
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: 62.38 E-value: 6.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 314 DGQITAILDQKNYVEELNRHLN---ATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESSyILESNRKG 390
Cdd:TIGR02168 666 AKTNSSILERRREIEELEEKIEeleEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLA-RLEAEVEQ 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 391 PKQDRTAEGQALSEARKHLKEETQLRLDVEKELEMQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAF 470
Cdd:TIGR02168 745 LEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRE 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 471 KLQSSDLGVKQKSELNSRLEEKTNQMAATIKQLEQRLRQAERSR--QSAELDNRLFKQDFGDK-INSLQLEVEELTRQRN 547
Cdd:TIGR02168 825 RLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIeeLESELEALLNERASLEEaLALLRSELEELSEELR 904
|
250
....*....|....*...
gi 767931431 548 QLELElKQEKERRLQNDR 565
Cdd:TIGR02168 905 ELESK-RSELRRELEELR 921
|
|
| RUN_RUBCN |
cd17686 |
RUN domain found in Run domain Beclin-1-interacting and cysteine-rich domain-containing ... |
148-281 |
9.03e-10 |
|
RUN domain found in Run domain Beclin-1-interacting and cysteine-rich domain-containing protein (RUBCN) and similar proteins; RUBCN, also called rubicon, or beclin-1 associated RUN domain containing protein (Baron), is part of a Beclin-1-Vps34-containing autophagy complex. It negatively regulates endosome maturation and degradative endocytic trafficking and impairs autophagosome maturation process. It is also an important negative regulator of the innate immune response, enhances viral replication and may play a role in viral immune evasion. This model contains the RUN domain of RUBCN.
Pssm-ID: 439048 Cd Length: 151 Bit Score: 57.28 E-value: 9.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 148 LNLGRTLD--SDYAPLQQFFVVMEHCLKHGLKAKKTFLGQNkSFWGPLELVEKLVPEAAEITASVKDLPGLKTPVG-RGR 224
Cdd:cd17686 6 LLLSRSSNvwSTYGGLQRLCRAVENILQHGLKEFQGLNKEI-DDWEFVQGLRWLQPTLAPSIEQQSRSSPSESEVSdKGR 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 767931431 225 AWLRLALMQKKLSEYMKALINKKELLSEFYEPNALMMEEEGAiiAGLLVGLNVIDAN 281
Cdd:cd17686 85 LWLRQSLQQHCLSSQLQWLVSDKELLRKYYEDEAFLRQEGYA--TALLICLTAVELN 139
|
|
| RUN1_DENND5B |
cd17691 |
RUN1 domain found in DENN domain-containing protein 5B (DENND5B) and similar proteins; DENND5B, ... |
210-283 |
2.08e-08 |
|
RUN1 domain found in DENN domain-containing protein 5B (DENND5B) and similar proteins; DENND5B, also called Rab6-interacting protein 1 (Rab6IP1)-like protein, functions in membrane trafficking at a crossroads between the Golgi and the endosomal system. It is composed of an N-terminal DENN (Differentially Expressed in Normal and Neoplastic cells) domain followed by two RUN (RPIP8 [RaP2-interacting protein 8], UNC-14, and NESCA [new molecule containing SH3 at the carboxyl terminus]) domains flanking a PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain. This model represents the first RUN domain of DENND5B.
Pssm-ID: 439053 [Multi-domain] Cd Length: 206 Bit Score: 54.68 E-value: 2.08e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767931431 210 VKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINKKELLSEFYEPNA-LMMEEEGAIIAGLLVGLNVIDAnFC 283
Cdd:cd17691 127 IQNMSEIKTDVGRARAWIRLSLEKKLLSQHLKQLLSNQALTKKLYKRYAfLRCEEEKEQFLYHLLSLNAVDY-FC 200
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
311-560 |
3.01e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.99 E-value: 3.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 311 TEGDGQITAILDQKNYVEELNRHLNATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEEssyilesnRKG 390
Cdd:TIGR02168 757 TELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRER--------LES 828
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 391 PKQDRTAEGQALSEARKHLKEETQLRLDVEKELEMQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAF 470
Cdd:TIGR02168 829 LERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELES 908
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 471 KLQSSDLGVKQKSELNSRLEEKTNQMAATIKQLEQRLrqaeRSRQSAELDNRL-FKQDFGDKINSLQLEVEELTRQRNQL 549
Cdd:TIGR02168 909 KRSELRRELEELREKLAQLELRLEGLEVRIDNLQERL----SEEYSLTLEEAEaLENKIEDDEEEARRRLKRLENKIKEL 984
|
250
....*....|....*...
gi 767931431 550 -------ELELKQEKERR 560
Cdd:TIGR02168 985 gpvnlaaIEEYEELKERY 1002
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
324-550 |
7.65e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 55.45 E-value: 7.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 324 KNYVEELNRhLNATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESSYILESNRKGpKQDRTAEGQALS 403
Cdd:TIGR02168 263 QELEEKLEE-LRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEEL-ESKLDELAEELA 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 404 EARKHLKEETQLRLDVEKELEMQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRA-----------LKHELAFKL 472
Cdd:TIGR02168 341 ELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNeierlearlerLEDRRERLQ 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 473 Q-----SSDLGVKQKSELNSRLEEKTNQMAATIKQLEQRLRQAERSRQSAELDNRLFkQDFGDKINSLQLEVEELTRQRN 547
Cdd:TIGR02168 421 QeieelLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQAL-DAAERELAQLQARLDSLERLQE 499
|
...
gi 767931431 548 QLE 550
Cdd:TIGR02168 500 NLE 502
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
369-566 |
1.27e-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: 54.69 E-value: 1.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 369 LQEEMERVKEESsYILESNRKGPKQDRTAEGQALSEARKHLKEETQLRLDVEKELEMQISMRQEMELAMKMLEKDVCEKQ 448
Cdd:TIGR02169 672 EPAELQRLRERL-EGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLE 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 449 DALVSLRQQLDDLRALKHEL-----AFKLQSSDLG-----------VKQKSELN---SRLEEKTNQMAATIKQLEQRLRQ 509
Cdd:TIGR02169 751 QEIENVKSELKELEARIEELeedlhKLEEALNDLEarlshsripeiQAELSKLEeevSRIEARLREIEQKLNRLTLEKEY 830
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767931431 510 AERSRQSAELDNRLFK---QDFGDKINSLQLEVEELTRQRNQLELELKQEKERR--LQNDRS 566
Cdd:TIGR02169 831 LEKEIQELQEQRIDLKeqiKSIEKEIENLNGKKEELEEELEELEAALRDLESRLgdLKKERD 892
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
342-567 |
3.29e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.38 E-value: 3.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 342 QAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESSYILESNRKGPKQDRTA----EGQALSEARKHLkEETQLRL 417
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVAsaerEIAELEAELERL-DASSDDL 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 418 dveKELEMQIsmrQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKLQssDLGVKQKSELNSRLEEK----- 492
Cdd:COG4913 688 ---AALEEQL---EELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLE--AAEDLARLELRALLEERfaaal 759
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 493 -TNQMAATIKQLEQRLRQAERSRQSAEldNRL------FKQDFGDKINSLQLEVEELT---RQRNQLE---LELKQEKER 559
Cdd:COG4913 760 gDAVERELRENLEERIDALRARLNRAE--EELeramraFNREWPAETADLDADLESLPeylALLDRLEedgLPEYEERFK 837
|
....*...
gi 767931431 560 RLQNDRSI 567
Cdd:COG4913 838 ELLNENSI 845
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
316-518 |
3.44e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.40 E-value: 3.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 316 QITAILDQKNYVEELNRHLNATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEEssyilesnRKGPKQDR 395
Cdd:COG1196 296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAE--------LAEAEEAL 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 396 TAEGQALSEARKHLKEETQLRLDVEKELEMQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKLQSS 475
Cdd:COG1196 368 LEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEA 447
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 767931431 476 DLGVKQKSELNSRLEEKTNQMAATIKQLEQRLRQAERSRQSAE 518
Cdd:COG1196 448 AEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAA 490
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
428-555 |
8.16e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.22 E-value: 8.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 428 SMRQEMELA---MKMLEkDVCEKQDALVSLRQQLDDLRALKHELA--FKLQSSDLGVKQKSELNSRLEEKTNQMA---AT 499
Cdd:COG4913 239 RAHEALEDAreqIELLE-PIRELAERYAAARERLAELEYLRAALRlwFAQRRLELLEAELEELRAELARLEAELErleAR 317
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 767931431 500 IKQLEQRLRQAERSRQSAEldnrlfkqdfGDKINSLQLEVEELTRQRNQLELELKQ 555
Cdd:COG4913 318 LDALREELDELEAQIRGNG----------GDRLEQLEREIERLERELEERERRRAR 363
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
328-560 |
9.34e-07 |
|
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: 51.94 E-value: 9.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 328 EELNRHLNATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESSYILESNRKGPKQDRTAEG-------- 399
Cdd:TIGR04523 210 IQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKkikelekq 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 400 -------------QALSEARKHLKEETQLRLDVEKELEMQISMRQ----EMELAMKMLEKDVCEKQDALVSLRQQL---- 458
Cdd:TIGR04523 290 lnqlkseisdlnnQKEQDWNKELKSELKNQEKKLEEIQNQISQNNkiisQLNEQISQLKKELTNSESENSEKQRELeekq 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 459 DDLRALKHELAFKLQSSDLGVKQKSELNSRLEEKTNQMaatiKQLEQRLRQAERSRQSAELDNRLFKQDfgdkINSLQLE 538
Cdd:TIGR04523 370 NEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLN----QQKDEQIKKLQQEKELLEKEIERLKET----IIKNNSE 441
|
250 260
....*....|....*....|..
gi 767931431 539 VEELTRQRNQLELELKQEKERR 560
Cdd:TIGR04523 442 IKDLTNQDSVKELIIKNLDNTR 463
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
337-562 |
1.06e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.60 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 337 TVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESSYILESNRKGPKQDRTAEgqalSEARKHLKEETQLR 416
Cdd:PRK03918 385 TPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELT----EEHRKELLEEYTAE 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 417 L-DVEKELEMQISMRQEMELAMKMLEKdVCEKQDALVSLRQQLDDLRALKHELAfKLQSSDLgvKQKSELNSRLEEKTNQ 495
Cdd:PRK03918 461 LkRIEKELKEIEEKERKLRKELRELEK-VLKKESELIKLKELAEQLKELEEKLK-KYNLEEL--EKKAEEYEKLKEKLIK 536
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767931431 496 MAATIKQLEQRLRQAErsrqsaELDNRLFKQDfgDKINSLQLEVEELTRQRNQLELELKQEKERRLQ 562
Cdd:PRK03918 537 LKGEIKSLKKELEKLE------ELKKKLAELE--KKLDELEEELAELLKELEELGFESVEELEERLK 595
|
|
| RUN_SGSM1 |
cd17703 |
RUN domain found in small G protein signaling modulator 1 (SGSM1) and similar proteins; SGSM1, ... |
140-274 |
1.33e-06 |
|
RUN domain found in small G protein signaling modulator 1 (SGSM1) and similar proteins; SGSM1, also called RUN and TBC1 domain-containing protein 2 (RUTBC2), interacts with numerous Rab family members, functioning as Rab effector for some, and as GTPase activator for others. It is a Rab9A effector and GTPase-activating protein for Rab36, and links Rab9A function to Rab36 function in the endosomal system. This model contains the RUN domain of SGSM1.
Pssm-ID: 439065 Cd Length: 177 Bit Score: 48.85 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 140 IKGLIESALNLgRTLDSDYAPLQQFFVVMEHCLKHGLKAKKT-FLGQNK----------SFWGPLELVEKL--------- 199
Cdd:cd17703 3 VKQIMEEAVTR-KFVHEDSSHIISFCAAVEACVLHGLKRRAAgFLRSNKiaalfmkvgkSFPPAEELCRKVqeleqllen 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 200 ----VPEAAEITASVKDLPGLkTPVGRGRAWLRLALMQKKLSEYMKALInkkELLSEFYEPNALMMEE-EGAIIAGLLVG 274
Cdd:cd17703 82 krnqMQGLQENVRKMPKLPNL-SPQAIKHLWIRTALFEKVLDKIVHYLV---ENSSKYYEKEALLMDPvDGPILASLLVG 157
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
402-562 |
1.54e-06 |
|
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: 51.49 E-value: 1.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 402 LSEARKHLKEETQLRLDVEKELEMQISMRQEMELAMKMLEKDV--CEKQDALVSLRQQLDDLRALKHelafklqssdlgv 479
Cdd:COG3096 443 LAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELVCKIAgeVERSQAWQTARELLRRYRSQQA------------- 509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 480 kqkselnsrLEEKTNQMAATIKQLEQRLRQAERSRQSAELDNRLFKQDFGDKINsLQLEVEELTRQRNQLELELKQEKER 559
Cdd:COG3096 510 ---------LAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEE-LEELLAELEAQLEELEEQAAEAVEQ 579
|
...
gi 767931431 560 RLQ 562
Cdd:COG3096 580 RSE 582
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
327-549 |
1.81e-06 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 51.07 E-value: 1.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 327 VEELNRHLNATVNNLQakvdaleksntKLTEELAVANNRIITLQEEMERVKEESSY----------ILESNRKGPKQDR- 395
Cdd:PRK11281 123 LRQLESRLAQTLDQLQ-----------NAQNDLAEYNSQLVSLQTQPERAQAALYAnsqrlqqirnLLKGGKVGGKALRp 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 396 ------TAEgQALSEA-----RKHLKEETQL------RLDVEKE----LEMQISMRQEM--ELAMKMLEKDVCEKQDALV 452
Cdd:PRK11281 192 sqrvllQAE-QALLNAqndlqRKSLEGNTQLqdllqkQRDYLTAriqrLEHQLQLLQEAinSKRLTLSEKTVQEAQSQDE 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 453 SLRQQLDDLraLKHELAFKLQSSDLGVKQKSELNSRLEEktNQMaatIKQLEQRLRQAERS--------RQSAELDNRLF 524
Cdd:PRK11281 271 AARIQANPL--VAQELEINLQLSQRLLKATEKLNTLTQQ--NLR---VKNWLDRLTQSERNikeqisvlKGSLLLSRILY 343
|
250 260 270
....*....|....*....|....*....|....*.
gi 767931431 525 KQ-----------DFGDKINSLQLEVEELTRQRNQL 549
Cdd:PRK11281 344 QQqqalpsadlieGLADRIADLRLEQFEINQQRDAL 379
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
312-574 |
1.96e-06 |
|
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: 50.84 E-value: 1.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 312 EGDGQITAILDQKNYVEELNRHLNATVNNLQAKVDALEKSNTKLTEElavannRIITLQEEMERVKEESSYILESNRKGP 391
Cdd:TIGR02169 241 AIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEE------EQLRVKEKIGELEAEIASLERSIAEKE 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 392 KQDRTAEGQA----------LSEARKHLKEETQLRLDVEKELEMQISMRQEMELAMKMLE---KDVCEKQDALVSLRQQL 458
Cdd:TIGR02169 315 RELEDAEERLakleaeidklLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEevdKEFAETRDELKDYREKL 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 459 DDLralKHELAFKLQSSDLGVKQKSELNSRL----------EEKTNQMAATIKQLEQRLRQAERSRQSAELDnrlfKQDF 528
Cdd:TIGR02169 395 EKL---KREINELKRELDRLQEELQRLSEELadlnaaiagiEAKINELEEEKEDKALEIKKQEWKLEQLAAD----LSKY 467
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 767931431 529 GDKINSLQLEVEELTRQRNQLELELKQ-EKERRLQNDRSIPGRGSQK 574
Cdd:TIGR02169 468 EQELYDLKEEYDRVEKELSKLQRELAEaEAQARASEERVRGGRAVEE 514
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
334-554 |
3.03e-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: 50.40 E-value: 3.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 334 LNATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEES----SYILESNRKGPKQDRTAegQALSEARKHL 409
Cdd:TIGR04523 340 LNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIknleSQINDLESKIQNQEKLN--QQKDEQIKKL 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 410 KEETQLrldVEKELEMQISMRQEMELAMKMLEKDVCEKQDALVSL-------RQQLDDL----RALKHELAFKLQSSDLG 478
Cdd:TIGR04523 418 QQEKEL---LEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLdntreslETQLKVLsrsiNKIKQNLEQKQKELKSK 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 479 VKQKSELN---SRLEEKTNQMAATIKQLEQRLRQ-----AERSRQSAELDNRLFKQDFGDKINSLQLEVEELTRQRNQLE 550
Cdd:TIGR04523 495 EKELKKLNeekKELEEKVKDLTKKISSLKEKIEKlesekKEKESKISDLEDELNKDDFELKKENLEKEIDEKNKEIEELK 574
|
....
gi 767931431 551 LELK 554
Cdd:TIGR04523 575 QTQK 578
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
315-559 |
4.67e-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: 48.99 E-value: 4.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 315 GQITAILDQKNYVEELNRHLNAtvnnLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESSyILESNRKGPKQD 394
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAE----LEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELA-ALEAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 395 RTAEGQALSEARKHLKEE--TQLRLDVEKELEMQISMR--QEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAF 470
Cdd:COG4942 92 IAELRAELEAQKEELAELlrALYRLGRQPPLALLLSPEdfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 471 KLQssdlgvkQKSELNSRLEEKTNQMAATIKQLEQRLRQAERSRQSAEldnrlfkqdfgDKINSLQLEVEELTRQRNQLE 550
Cdd:COG4942 172 ERA-------ELEALLAELEEERAALEALKAERQKLLARLEKELAELA-----------AELAELQQEAEELEALIARLE 233
|
....*....
gi 767931431 551 LELKQEKER 559
Cdd:COG4942 234 AEAAAAAER 242
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
302-584 |
6.10e-06 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 49.35 E-value: 6.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 302 LKDGNSSKGTEGDGQITAILDQKNYVEELNRHLNATvnNLQAKVDALEKSNTkltEELAVANNRIITL-------QEEME 374
Cdd:pfam17380 318 LEEAEKARQAEMDRQAAIYAEQERMAMERERELERI--RQEERKRELERIRQ---EEIAMEISRMRELerlqmerQQKNE 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 375 RVKEE-----SSYILESNRKGPKQDRTAEGQALSEARKHLKEETQLRLDVEKELEMQISMRQEMELAMKM--LEKDVCEK 447
Cdd:pfam17380 393 RVRQEleaarKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVerLRQQEEER 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 448 QDALVSLRQQLDDlRALKHELAFKLQSSDLGVKQKS---ELNSR--LEEKTNQMAATIKQLEQRLRQAERSRQSAELDNR 522
Cdd:pfam17380 473 KRKKLELEKEKRD-RKRAEEQRRKILEKELEERKQAmieEERKRklLEKEMEERQKAIYEEERRREAEEERRKQQEMEER 551
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767931431 523 lfkqdfgdkiNSLQLEVEELTRQRNQLElelKQEKERRLQndRSIPGRGSQKSESKmAATPP 584
Cdd:pfam17380 552 ----------RRIQEQMRKATEERSRLE---AMEREREMM--RQIVESEKARAEYE-ATTPI 597
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
329-565 |
6.69e-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: 49.33 E-value: 6.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 329 ELNRHLNATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESSYILESNRKGPKQDRTA----EGQALSE 404
Cdd:pfam05483 289 EKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATtcslEELLRTE 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 405 ARKHLKEETQLRL---DVEK---ELEMQISMRQEMELAMKMLEKDVCEKQDALVSLRQ---QLDDLRALKHELAFKLQSS 475
Cdd:pfam05483 369 QQRLEKNEDQLKIitmELQKkssELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQfekIAEELKGKEQELIFLLQAR 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 476 DlgvKQKSELNSrleektnQMAATIKQLEQRLRQAERSRqsAELDNRLFKQ-DFGDKINSLQLEVEELTRQRNQLELELK 554
Cdd:pfam05483 449 E---KEIHDLEI-------QLTAIKTSEEHYLKEVEDLK--TELEKEKLKNiELTAHCDKLLLENKELTQEASDMTLELK 516
|
250
....*....|.
gi 767931431 555 QEKERRLQNDR 565
Cdd:pfam05483 517 KHQEDIINCKK 527
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
328-558 |
1.55e-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: 48.25 E-value: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 328 EELNRHLNATVNNLQAKVDALEKsntKLTEELAvANNRI----ITLQEEMERVKEESSYILESNRKGPKQDRTAEgQALS 403
Cdd:pfam01576 88 EERSQQLQNEKKKMQQHIQDLEE---QLDEEEA-ARQKLqlekVTTEAKIKKLEEDILLLEDQNSKLSKERKLLE-ERIS 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 404 EARKHLKEE-------TQLRL-------DVEKELEMQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELA 469
Cdd:pfam01576 163 EFTSNLAEEeekakslSKLKNkheamisDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKE 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 470 FKLQSSDLGVKQKSELNSRLEEKTNQMAATIKQLEQRLRQAERSRQSAELDNRlfkqDFGDKINSLQLEVEE-LTRQRNQ 548
Cdd:pfam01576 243 EELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRR----DLGEELEALKTELEDtLDTTAAQ 318
|
250
....*....|
gi 767931431 549 LELELKQEKE 558
Cdd:pfam01576 319 QELRSKREQE 328
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
395-567 |
1.79e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.01 E-value: 1.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 395 RTAEGQALSEARKHLKEETQLRLDVEKELEMQIsmrQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKLQS 474
Cdd:COG1196 223 KELEAELLLLKLRELEAELEELEAELEELEAEL---EELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELAR 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 475 SDLGVKQKSELNSRLEEKTNQMAATIKQLEQRLRQAERSRQSAELDNRLFKQDFGDKINSL---QLEVEELTRQRNQLEL 551
Cdd:COG1196 300 LEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELaeaEEALLEAEAELAEAEE 379
|
170
....*....|....*.
gi 767931431 552 ELKQEKERRLQNDRSI 567
Cdd:COG1196 380 ELEELAEELLEALRAA 395
|
|
| RUN1_DENND5A |
cd17690 |
RUN1 domain found in DENN domain-containing protein 5A (DENND5A) and similar proteins; DENND5A, ... |
210-283 |
2.06e-05 |
|
RUN1 domain found in DENN domain-containing protein 5A (DENND5A) and similar proteins; DENND5A, also called Rab6-interacting protein 1 (Rab6IP1), is present predominantly in developing neuronal tissue, and functions in membrane trafficking at a crossroads between the Golgi and the endosomal system. It is composed of an N-terminal DENN (Differentially Expressed in Normal and Neoplastic cells) domain followed by two RUN (RPIP8 [RaP2-interacting protein 8], UNC-14, and NESCA [new molecule containing SH3 at the carboxyl terminus]) domains flanking a PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain. This model represents the first RUN domain of DENND5A.
Pssm-ID: 439052 [Multi-domain] Cd Length: 209 Bit Score: 45.77 E-value: 2.06e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767931431 210 VKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINKKELLSEFYEPNA-LMMEEEGAIIAGLLVGLNVIDAnFC 283
Cdd:cd17690 130 IQNIGEIKTDVGKARAWVRLSMEKKLLSRHLKQLLSDHELTKKLYKRYAfLRCDDEKEQFLYHLLSFNAVDY-FC 203
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
322-498 |
2.13e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.13 E-value: 2.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 322 DQKNYVEELNRhLNATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEE------SSY-----------IL 384
Cdd:COG3883 31 ELEAAQAELDA-LQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREElgerarALYrsggsvsyldvLL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 385 ESnrKGPKQ--DR--------TAEGQALSEARKHLKEETQLRLDVEKELEMQISMRQEMELAMKMLEKDVCEKQDALVSL 454
Cdd:COG3883 110 GS--ESFSDflDRlsalskiaDADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQL 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 767931431 455 RQQLDDLRALKHELAFKLQSSDLGVKQKSELNSRLEEKTNQMAA 498
Cdd:COG3883 188 SAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAA 231
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
339-518 |
2.45e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 47.32 E-value: 2.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 339 NNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESSYILESNRKGPKQDRTAE-GQALSEARKHLKEETQLRL 417
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLSEEAKLLLQQLSElESQLAEARAELAEAEARLA 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 418 DVEKELEMQISM----------------RQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRA-LKHELAFKLQSSDLGVK 480
Cdd:COG3206 244 ALRAQLGSGPDAlpellqspviqqlraqLAELEAELAELSARYTPNHPDVIALRAQIAALRAqLQQEAQRILASLEAELE 323
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 767931431 481 ----QKSELNSRLEEkTNQMAATIKQLEQRLRQAERSRQSAE 518
Cdd:COG3206 324 alqaREASLQAQLAQ-LEARLAELPELEAELRRLEREVEVAR 364
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
5-100 |
4.03e-05 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 46.86 E-value: 4.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 5 PPPPTAGAESCSEEPARGGEWRPEEPRRAPAGGTDREGEAGPPPASPAGQSEPD-SPVAAPffllYPGDGGAGFGVrPPP 83
Cdd:PHA03247 2829 PPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARPPvRRLARP----AVSRSTESFAL-PPD 2903
|
90
....*....|....*..
gi 767931431 84 QQQRSwRTPPSPGSPLP 100
Cdd:PHA03247 2904 QPERP-PQPQAPPPPQP 2919
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
320-552 |
6.20e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 46.21 E-value: 6.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 320 ILDQK--NYVEELnRHLNATVNNLQAKVDALEKSNTKLTEELAvaNNRIITLQEEMERVKEESSYILESNR--KGPKQDR 395
Cdd:TIGR02169 748 SLEQEieNVKSEL-KELEARIEELEEDLHKLEEALNDLEARLS--HSRIPEIQAELSKLEEEVSRIEARLReiEQKLNRL 824
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 396 TAEGQALSEARKHLKE---ETQLRL-DVEKELEMQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFK 471
Cdd:TIGR02169 825 TLEKEYLEKEIQELQEqriDLKEQIkSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERK 904
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 472 LQssdlgvKQKSELNsRLEEKTNQMAATIKQLEQRLRQAErsrqsaeldnRLFKQDFGDKINSLQLEVEELTRQRNQLEL 551
Cdd:TIGR02169 905 IE------ELEAQIE-KKRKRLSELKAKLEALEEELSEIE----------DPKGEDEEIPEEELSLEDVQAELQRVEEEI 967
|
.
gi 767931431 552 E 552
Cdd:TIGR02169 968 R 968
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
373-560 |
6.54e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.91 E-value: 6.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 373 MERVKEESSYILESNRKGPKQDRTaEGQALSEARKHLKEETQLRLDVEKELEMQISMRQEMELAMKMLEKDVcEKQDALV 452
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLK-ELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREEL-EKLEKLL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 453 SLRQQLDDLRALKHELAfklqssdlgvkqksELNSRLEEKTNQMAA---TIKQLEQRLRQAERSRQSAELDNRLFKQDFG 529
Cdd:COG4717 126 QLLPLYQELEALEAELA--------------ELPERLEELEERLEElreLEEELEELEAELAELQEELEELLEQLSLATE 191
|
170 180 190
....*....|....*....|....*....|.
gi 767931431 530 DKINSLQLEVEELTRQRNQLELELKQEKERR 560
Cdd:COG4717 192 EELQDLAEELEELQQRLAELEEELEEAQEEL 222
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
328-557 |
7.46e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 45.88 E-value: 7.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 328 EELNRHLNATVNNLQA----KVDALEKSNTKLtEELavannRIITLQEEmeRVKEESSYIL-----ESNRKGPKQDRTAE 398
Cdd:pfam15921 141 EDLRNQLQNTVHELEAakclKEDMLEDSNTQI-EQL-----RKMMLSHE--GVLQEIRSILvdfeeASGKKIYEHDSMST 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 399 ------GQALSEARKHLKEETQLR----LDVEKELEMQISMRQ-EMELAMKM----LEKDVCEKQDALVSLRQQLDDLRA 463
Cdd:pfam15921 213 mhfrslGSAISKILRELDTEISYLkgriFPVEDQLEALKSESQnKIELLLQQhqdrIEQLISEHEVEITGLTEKASSARS 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 464 LKHELAFKLQssdLGVKQKSELNSRLEEKTNQMAATIKQLEQRLRQAERSRQSA--ELDNRL----------------FK 525
Cdd:pfam15921 293 QANSIQSQLE---IIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKieELEKQLvlanseltearterdqFS 369
|
250 260 270
....*....|....*....|....*....|..
gi 767931431 526 QDFGDKINSLQLEVEELTRQRNQLELELKQEK 557
Cdd:pfam15921 370 QESGNLDDQLQKLLADLHKREKELSLEKEQNK 401
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
314-555 |
8.02e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 45.82 E-value: 8.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 314 DGQITAILDQKNYVEELNRHLNATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEEssyiLESNRKGPKQ 393
Cdd:TIGR02168 301 EQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAE----LEELESRLEE 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 394 DRTAEGQALSEARKHLKEETQLRLDV---EKELEMQISMRQEM-----ELAMKMLEKDVCEkqdalvsLRQQLDDLRALK 465
Cdd:TIGR02168 377 LEEQLETLRSKVAQLELQIASLNNEIerlEARLERLEDRRERLqqeieELLKKLEEAELKE-------LQAELEELEEEL 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 466 HELafklqssdlgVKQKSELNSRLEEKTNQmaatIKQLEQRLRQAErsRQSAELDNRLfkqdfgDKINSLQLEVEELTRQ 545
Cdd:TIGR02168 450 EEL----------QEELERLEEALEELREE----LEEAEQALDAAE--RELAQLQARL------DSLERLQENLEGFSEG 507
|
250
....*....|
gi 767931431 546 RNQLELELKQ 555
Cdd:TIGR02168 508 VKALLKNQSG 517
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
413-563 |
1.05e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.75 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 413 TQLRLDVEKELEMQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKLQSSDlgvKQKSELNSRLEEK 492
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALE---AELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 493 TNQMAATIKQLEQRLRQAERSRQSAELDNRLFKQDFGD-----------------KINSLQLEVEELTRQRNQLELElKQ 555
Cdd:COG4942 96 RAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDavrrlqylkylaparreQAEELRADLAELAALRAELEAE-RA 174
|
....*...
gi 767931431 556 EKERRLQN 563
Cdd:COG4942 175 ELEALLAE 182
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
400-556 |
1.37e-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: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 400 QALSEARKHLKEETQLRLDVEKELEMQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLD------DLRALKHELAF-KL 472
Cdd:COG1579 24 HRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGnvrnnkEYEALQKEIESlKR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 473 QSSDLGvKQKSELNSRLEEKTNQMAATIKQLEQRlrQAERSRQSAELDnrlfkqdfgDKINSLQLEVEELTRQRNQLELE 552
Cdd:COG1579 104 RISDLE-DEILELMERIEELEEELAELEAELAEL--EAELEEKKAELD---------EELAELEAELEELEAEREELAAK 171
|
....
gi 767931431 553 LKQE 556
Cdd:COG1579 172 IPPE 175
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
327-506 |
1.47e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 44.83 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 327 VEELNRHLNATVNNL----QAKVDA---LEKSNTKLTEELAVANNRIITLQEEMERVKEesSYIL-----ESNRKGPKQ- 393
Cdd:PRK04778 280 AEEKNEEIQERIDQLydilEREVKArkyVEKNSDTLPDFLEHAKEQNKELKEEIDRVKQ--SYTLneselESVRQLEKQl 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 394 -----------DRTAEG-QALSEARKHLKE-ETQLRlDVEKElemQISMRQEmelaMKMLEKDvcEKQdalvsLRQQLDD 460
Cdd:PRK04778 358 eslekqydeitERIAEQeIAYSELQEELEEiLKQLE-EIEKE---QEKLSEM----LQGLRKD--ELE-----AREKLER 422
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 767931431 461 LRALKHELAFKLQSSDL-GVKQksELNSRLEEKTNQMAATIKQLEQR 506
Cdd:PRK04778 423 YRNKLHEIKRYLEKSNLpGLPE--DYLEMFFEVSDEIEALAEELEEK 467
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
402-568 |
1.48e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.95 E-value: 1.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 402 LSEARKHLKEETQLRLDVEKELEMQISMRQEMELAMKMLEK--DVCEKQDALVSLRQQLDDLRALKHeLAFKLQssdlGV 479
Cdd:PRK04863 444 LEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKiaGEVSRSEAWDVARELLRRLREQRH-LAEQLQ----QL 518
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 480 KQK-SELNSRLEEKtnqmaatiKQLEQRLRQAERsRQSAELDNRLFKQDF----GDKINSLQLEVEELTRQRNQLELELK 554
Cdd:PRK04863 519 RMRlSELEQRLRQQ--------QRAERLLAEFCK-RLGKNLDDEDELEQLqeelEARLESLSESVSEARERRMALRQQLE 589
|
170
....*....|....
gi 767931431 555 QEKERRLQNDRSIP 568
Cdd:PRK04863 590 QLQARIQRLAARAP 603
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
328-563 |
1.86e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.67 E-value: 1.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 328 EELNRHLNATVNNLQAKVDALEKSntklTEELAVANNRIITLQEEMERVKEESSYIL-ESNRKGPKQDRTAEGQaLSEAR 406
Cdd:PRK03918 524 AEEYEKLKEKLIKLKGEIKSLKKE----LEKLEELKKKLAELEKKLDELEEELAELLkELEELGFESVEELEER-LKELE 598
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 407 KHLKEETQLRlDVEKELEMQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKlqssdlgvkqkseln 486
Cdd:PRK03918 599 PFYNEYLELK-DAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYE--------------- 662
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767931431 487 sRLEEKTNQMAATIKQLEQRLRQAERSRQSAELDNRLFKQDFgDKINSLQLEVEELTRQRNQLElELKqEKERRLQN 563
Cdd:PRK03918 663 -ELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEEL-EEREKAKKELEKLEKALERVE-ELR-EKVKKYKA 735
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
337-552 |
1.87e-04 |
|
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: 43.59 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 337 TVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESSYILESNRkgpkqdrtaegQALSEARKHLKEETQLR 416
Cdd:pfam09787 41 SSTALTLELEELRQERDLLREEIQKLRGQIQQLRTELQELEAQQQEEAESSR-----------EQLQELEEQLATERSAR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 417 LDVEKELEmqiSMRQEMElamKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKLQSSdlgvKQKSELNSRLEEKTNQM 496
Cdd:pfam09787 110 REAEAELE---RLQEELR---YLEEELRRSKATLQSRIKDREAEIEKLRNQLTSKSQSS----SSQSELENRLHQLTETL 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 767931431 497 AATIKQLEQrlRQAERsrqsaeldnrlfkqdfgdkiNSLQLEVEELTRQRNQLELE 552
Cdd:pfam09787 180 IQKQTMLEA--LSTEK--------------------NSLVLQLERMEQQIKELQGE 213
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
316-562 |
1.91e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 44.57 E-value: 1.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 316 QITAILDQknyvEELNRHLNATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESSYILesnrkgpkQDR 395
Cdd:TIGR00618 387 QKTTLTQK----LQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTA--------QCE 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 396 TAEGQALSEARKHLKEETQLRLDVEKELEMQISMRQEME---LAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKL 472
Cdd:TIGR00618 455 KLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLarlLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGE 534
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 473 QSSDLGVKQKSELNSRLEEKTNQmAATIKQLEQRLRQAE------RSRQSAELDNRLFKQDFGDKINSLQLEVEELTRQR 546
Cdd:TIGR00618 535 QTYAQLETSEEDVYHQLTSERKQ-RASLKEQMQEIQQSFsiltqcDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACE 613
|
250
....*....|....*.
gi 767931431 547 NQLELELKQEKERRLQ 562
Cdd:TIGR00618 614 QHALLRKLQPEQDLQD 629
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
338-557 |
2.27e-04 |
|
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: 44.18 E-value: 2.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 338 VNNLQAKVDALEKSNTKLTEELAVANNriiTLQEEMERVKEESSYILESNRKGPKQDR-TAEGQALSEARKHLKEETQLR 416
Cdd:COG5185 324 EQELEESKRETETGIQNLTAEIEQGQE---SLTENLEAIKEEIENIVGEVELSKSSEElDSFKDTIESTKESLDEIPQNQ 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 417 LDVEKELEMQIsmrqemELAMKMLEKDVCEKQDALVSLRQQLDD----LRALKHELAFKLQSSDLGVKQK-----SELNS 487
Cdd:COG5185 401 RGYAQEILATL------EDTLKAADRQIEELQRQIEQATSSNEEvsklLNELISELNKVMREADEESQSRleeayDEINR 474
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767931431 488 RLEEKTNQMAATIKQLEQRLR--QAERSRQSAELDNRLfkQDFGDKINSLQLEVEELTRQRNQLELELKQEK 557
Cdd:COG5185 475 SVRSKKEDLNEELTQIESRVStlKATLEKLRAKLERQL--EGVRSKLDQVAESLKDFMRARGYAHILALENL 544
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
2-100 |
2.46e-04 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 44.21 E-value: 2.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 2 AETPPPPTAGAESCSEEPARGGewRPEEPRRAPAGGTDREGEAGPPPASPAGQSEPDSPVAAPFflLYPGDGGAGFGVRP 81
Cdd:PRK07764 598 EGPPAPASSGPPEEAARPAAPA--APAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAV--PDASDGGDGWPAKA 673
|
90
....*....|....*....
gi 767931431 82 PPQQQRSWRTPPSPGSPLP 100
Cdd:PRK07764 674 GGAAPAAPPPAPAPAAPAA 692
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
338-562 |
3.21e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.60 E-value: 3.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 338 VNNLQAKVDALEKSNTKLTE----ELAVANNRIITLQEEMERVKEEssyilesnrkgpKQDRTAEGQALSEARKHLKEET 413
Cdd:COG4717 48 LERLEKEADELFKPQGRKPElnlkELKELEEELKEAEEKEEEYAEL------------QEELEELEEELEELEAELEELR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 414 QLRLDVEKELEMQISMRQEMELAMKMLEKDVC--EKQDALVSLRQQLDDLRALKHELAfklqssdlgvKQKSELNSRLEE 491
Cdd:COG4717 116 EELEKLEKLLQLLPLYQELEALEAELAELPERleELEERLEELRELEEELEELEAELA----------ELQEELEELLEQ 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767931431 492 KTNQMAATIKQLEQRLRQAERSRQSAEldnrlfkqdfgDKINSLQLEVEELTRQRNQLELEL-KQEKERRLQ 562
Cdd:COG4717 186 LSLATEEELQDLAEELEELQQRLAELE-----------EELEEAQEELEELEEELEQLENELeAAALEERLK 246
|
|
| PHA03264 |
PHA03264 |
envelope glycoprotein D; Provisional |
3-100 |
3.54e-04 |
|
envelope glycoprotein D; Provisional
Pssm-ID: 223029 [Multi-domain] Cd Length: 416 Bit Score: 43.07 E-value: 3.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 3 ETPPPPTAGAescseePARGGEWRPeEPRRAPAGGTD----REGEAGPPPASPAGQ--SEPDSPVAAPFFLLYPGDGGAG 76
Cdd:PHA03264 265 EPPPAPSGGS------PAPPGDDRP-EAKPEPGPVEDgapgRETGGEGEGPEPAGRdgAAGGEPKPGPPRPAPDADRPEG 337
|
90 100
....*....|....*....|....
gi 767931431 77 FgvrppPQQQRSWRTPPSPGSPLP 100
Cdd:PHA03264 338 W-----PSLEAITFPPPTPATPAV 356
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
338-562 |
4.25e-04 |
|
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: 43.20 E-value: 4.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 338 VNNLQAKVDALEKSNTKL-------TEELAVANNRIITLQEEMERVKEE---SSYILESNRKG---------PKQDRTAE 398
Cdd:pfam07111 164 LSSLTSKAEGLEKSLNSLetkrageAKQLAEAQKEAELLRKQLSKTQEEleaQVTLVESLRKYvgeqvppevHSQTWELE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 399 GQALSEARKHLKEEtqlRLDVEKELEM-QISMR--------QEMELAMKMLEKDVCEKQDALvSLRQQLDDLRALKHELA 469
Cdd:pfam07111 244 RQELLDTMQHLQED---RADLQATVELlQVRVQslthmlalQEEELTRKIQPSDSLEPEFPK-KCRSLLNRWREKVFALM 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 470 FKLQSSDLgvkqkselnsrleektnQMAATIKQLEQRLRQAERSRQSAELDNRLFKQDFGDKinSLQLEVEELTRQRNQL 549
Cdd:pfam07111 320 VQLKAQDL-----------------EHRDSVKQLRGQVAELQEQVTSQSQEQAILQRALQDK--AAEVEVERMSAKGLQM 380
|
250
....*....|...
gi 767931431 550 ELELKQEKERRLQ 562
Cdd:pfam07111 381 ELSRAQEARRRQQ 393
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
332-557 |
4.51e-04 |
|
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: 43.17 E-value: 4.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 332 RHLNATVNNLQAKVDALEKSNTKLTeelavANNRIITLqEEMERVKEESSYILE--SNRKGPKQDRTAEGQALSEARKHL 409
Cdd:pfam05483 467 EHYLKEVEDLKTELEKEKLKNIELT-----AHCDKLLL-ENKELTQEASDMTLElkKHQEDIINCKKQEERMLKQIENLE 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 410 KEETQLRLDVEKELEMQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKLQSSDLGVKQKSELNSRL 489
Cdd:pfam05483 541 EKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKAL 620
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767931431 490 EEKTNQMAATIKQLEQRLRQAERSRQSAeldnrlfKQDFGDKINSLQLEVEELTRQRNQLELELKQEK 557
Cdd:pfam05483 621 KKKGSAENKQLNAYEIKVNKLELELASA-------KQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAK 681
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
431-559 |
6.43e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.51 E-value: 6.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 431 QEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKLQSSDlgvKQKSELNSRLEEKTNQMAATIKQLEQRLRQA 510
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQ---AEIDKLQAEIAEAEAEIEERREELGERARAL 95
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 767931431 511 ERSRQSAELDNRLFK-QDFGDKINSLQLeVEELTRQRNQLELELKQEKER 559
Cdd:COG3883 96 YRSGGSVSYLDVLLGsESFSDFLDRLSA-LSKIADADADLLEELKADKAE 144
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
5-100 |
6.50e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 43.00 E-value: 6.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 5 PPPPTAGAESCSEEPARGGEWRP--EEPRRAPAGGTDREGEAGPPPASPAGQSEPD---SPVAAPffllyPGDGGAGFGV 79
Cdd:PHA03247 2625 DPPPPSPSPAANEPDPHPPPTVPppERPRDDPAPGRVSRPRRARRLGRAAQASSPPqrpRRRAAR-----PTVGSLTSLA 2699
|
90 100
....*....|....*....|...
gi 767931431 80 RPPPQQQRSWRTPP--SPGSPLP 100
Cdd:PHA03247 2700 DPPPPPPTPEPAPHalVSATPLP 2722
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
353-560 |
6.78e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 42.74 E-value: 6.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 353 TKLTEELAVANNRIITLQEEMERVKEessyIL-ESNRKGPKQDRTAEgqaLSEARKHLKEE-TQLRLDVE-KELEMQISM 429
Cdd:TIGR02168 168 SKYKERRKETERKLERTRENLDRLED----ILnELERQLKSLERQAE---KAERYKELKAElRELELALLvLRLEELREE 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 430 RQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKLQSSDLGVKQKSELNSRLEEKtnqmaatIKQLEQRLRQ 509
Cdd:TIGR02168 241 LEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQ-------KQILRERLAN 313
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 767931431 510 AERSRQSAELDNRLFKQDFGDKINSLQLEVEELTRQRNQLELELKQEKERR 560
Cdd:TIGR02168 314 LERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELE 364
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
322-562 |
6.98e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 42.65 E-value: 6.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 322 DQKNYVEELNRHLNATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESSYILESNRKgPKQDRTAEGQA 401
Cdd:pfam02463 744 KIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELK-EEAELLEEEQL 822
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 402 LSEARKHLKEETQLRLDVEKELEM--QISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFK----LQSS 475
Cdd:pfam02463 823 LIEQEEKIKEEELEELALELKEEQklEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKekeeKKEL 902
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 476 DLGVKQKSELNSRLEEKTNQMAATIKQLEQRLRQAERSRQSAELDNRLFKQD---FGDKINSLQLEVEELTRQRNQLELE 552
Cdd:pfam02463 903 EEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNkeeEEERNKRLLLAKEELGKVNLMAIEE 982
|
250
....*....|
gi 767931431 553 LKQEKERRLQ 562
Cdd:pfam02463 983 FEEKEERYNK 992
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
480-563 |
7.35e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.46 E-value: 7.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 480 KQKSELNSRLEEKTNQmaatIKQLEQRLRQAER--SRQSAELDNRlfKQDFGDKINSLQLEVEELTRQRNQLElELKQEK 557
Cdd:PRK12704 68 KLRNEFEKELRERRNE----LQKLEKRLLQKEEnlDRKLELLEKR--EEELEKKEKELEQKQQELEKKEEELE-ELIEEQ 140
|
....*.
gi 767931431 558 ERRLQN 563
Cdd:PRK12704 141 LQELER 146
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
316-564 |
8.26e-04 |
|
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: 42.31 E-value: 8.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 316 QITAILDQKNYVEELNRHLNATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEEssyiLESNRKgpKQDR 395
Cdd:TIGR04523 69 KINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQ----KKENKK--NIDK 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 396 TaegqaLSEARkhlKEETQLRLDVEK--ELEMQIsmrQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKLQ 473
Cdd:TIGR04523 143 F-----LTEIK---KKEKELEKLNNKynDLKKQK---EELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQ 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 474 SSDLGVKQKSElnsrLEEKTNQMAATIKQLEQRL--RQAERSRQSAELDNRLFKQD-FGDKINSLQLEVE-------ELT 543
Cdd:TIGR04523 212 KNKSLESQISE----LKKQNNQLKDNIEKKQQEIneKTTEISNTQTQLNQLKDEQNkIKKQLSEKQKELEqnnkkikELE 287
|
250 260
....*....|....*....|....
gi 767931431 544 RQRNQLELE---LKQEKERRLQND 564
Cdd:TIGR04523 288 KQLNQLKSEisdLNNQKEQDWNKE 311
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
3-107 |
1.07e-03 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 42.08 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 3 ETPPPPTAGAESCSEEPARGGEW-----RPEEPRRAPAGGTD-REGEAGPPP-ASPAGQSEPDSPVAAPFFLLYPGDGGA 75
Cdd:PHA03307 68 PTGPPPGPGTEAPANESRSTPTWslstlAPASPAREGSPTPPgPSSPDPPPPtPPPASPPPSPAPDLSEMLRPVGSPGPP 147
|
90 100 110
....*....|....*....|....*....|..
gi 767931431 76 GFGVRPPPQQQRSWRTPPSPGSPLPFLLLSYP 107
Cdd:PHA03307 148 PAASPPAAGASPAAVASDAASSRQAALPLSSP 179
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
237-559 |
1.08e-03 |
|
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: 42.02 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 237 SEYMKALINKKELLSEFYEPNALMMEEEGAIIAGLLVGLNVIDANFCMKGEDLDSQvgvidfsmyLKDGNSSKGTEgDGQ 316
Cdd:pfam05483 281 DENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQ---------MEELNKAKAAH-SFV 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 317 ITAILDQKNYVEELNR----HLNATVNNLQAKVDALEKSNTKLTEELAVANNRIITLqEEMERVKEESSYILESNR---- 388
Cdd:pfam05483 351 VTEFEATTCSLEELLRteqqRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVEL-EELKKILAEDEKLLDEKKqfek 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 389 -----KGPKQDRTAEGQA---------------LSEARKHLKEETQLRLDVEKELEMQISMRQEMELAMKMLEKDVCEKQ 448
Cdd:pfam05483 430 iaeelKGKEQELIFLLQArekeihdleiqltaiKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEAS 509
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 449 DALVSLRQQLDDLRALKHELAFKLQSSDLGVKQKSELNSRLEEKTNQMAATIKQLEQRLRQAERSRQSAE---LDNRLFK 525
Cdd:pfam05483 510 DMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEyevLKKEKQM 589
|
330 340 350
....*....|....*....|....*....|....
gi 767931431 526 QDFGDKINSLQLEVEELTRQRNQLELELKQEKER 559
Cdd:pfam05483 590 KILENKCNNLKKQIENKNKNIEELHQENKALKKK 623
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
348-567 |
1.12e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.43 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 348 LEKSNTKLTEELAVANNRIITLQEEMERVKEESSYiLESNRKGPKQDRTAEGQALSEARKHLKEETQLRLDVEKELEMQI 427
Cdd:COG4372 15 LFGLRPKTGILIAALSEQLRKALFELDKLQEELEQ-LREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 428 SMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKLQSSDLGVKQKSELNSRLEEKTNQMAATIKQLEQRL 507
Cdd:COG4372 94 AELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQEL 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767931431 508 RQAERSRQSAELDNRL-----FKQDFGDKINSLQLEVEELTRQRNQLELELKQEKERRLQNDRSI 567
Cdd:COG4372 174 QALSEAEAEQALDELLkeanrNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSAL 238
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
330-510 |
1.12e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 41.96 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 330 LNRHLNATVNNLQAKVDALEK--SNTKLTEELAVANNRII----TLQEEMERVKEESSYI----------------LESN 387
Cdd:PRK10929 80 LSAELRQQLNNERDEPRSVPPnmSTDALEQEILQVSSQLLeksrQAQQEQDRAREISDSLsqlpqqqtearrqlneIERR 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 388 RKGPKQDRTAEGQALSEARKhlKEETQLRLDVEkELEM-QISM--RQEM-ELAMKMLEKDVCEKQDALVSLRQQLDDLRA 463
Cdd:PRK10929 160 LQTLGTPNTPLAQAQLTALQ--AESAALKALVD-ELELaQLSAnnRQELaRLRSELAKKRSQQLDAYLQALRNQLNSQRQ 236
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 767931431 464 LKHELAFKL------QSSDL--GVKQKSELNSRLEEKTNQMAATIKQLEQRLRQA 510
Cdd:PRK10929 237 REAERALEStellaeQSGDLpkSIVAQFKINRELSQALNQQAQRMDLIASQQRQA 291
|
|
| DUF3729 |
pfam12526 |
Protein of unknown function (DUF3729); This family of proteins is found in viruses. Proteins ... |
9-107 |
1.13e-03 |
|
Protein of unknown function (DUF3729); This family of proteins is found in viruses. Proteins in this family are typically between 145 and 1707 amino acids in length. The family is found in association with pfam01443, pfam01661, pfam05417, pfam01660, pfam00978. There is a single completely conserved residue L that may be functionally important.
Pssm-ID: 372164 [Multi-domain] Cd Length: 115 Bit Score: 38.91 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 9 TAGAESCSE--EPARGGEWRPEEPRRAPAGGTDREGEAGPPPASPAGQSEPDSPvaapffllyPGDGGAGFGvrPPPqqq 86
Cdd:pfam12526 22 TSGFSSCFSppESAHPDPPPPVGDPRPPVVDTPPPVSAVWVLPPPSEPAAPEPD---------LVPPVTGPA--GPP--- 87
|
90 100
....*....|....*....|....*....
gi 767931431 87 rSWRTPPSPGSPLPF--------LLLSYP 107
Cdd:pfam12526 88 -SPLAPPAPAQKPPLppprpqrrLLHTYP 115
|
|
| PHA03201 |
PHA03201 |
uracil DNA glycosylase; Provisional |
12-98 |
1.34e-03 |
|
uracil DNA glycosylase; Provisional
Pssm-ID: 165468 Cd Length: 318 Bit Score: 41.03 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 12 AESCSEEPARggewRPEEPRRAPAGGTDREGEAGPP-PASPAGQSEPD--SPVAAPFFLLYPGDGGAGFGVRPPPQQQRS 88
Cdd:PHA03201 4 ARSRSPSPPR----RPSPPRPTPPRSPDASPEETPPsPPGPGAEPPPGraAGPAAPRRRPRGCPAGVTFSSSAPPRPPLG 79
|
90
....*....|
gi 767931431 89 WRTPPSPGSP 98
Cdd:PHA03201 80 LDDAPAATPP 89
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
341-526 |
1.43e-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: 40.68 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 341 LQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEEssyiLESNRkgpKQDRTAEGQaLSEARKHLKE-ETQLRL-- 417
Cdd:COG1579 15 LDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTE----LEDLE---KEIKRLELE-IEEVEARIKKyEEQLGNvr 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 418 ------DVEKELEMQismrqemELAMKMLEKDVCEKQDALVSLRQQLDDLRAlkhelafklqssdlgvkQKSELNSRLEE 491
Cdd:COG1579 87 nnkeyeALQKEIESL-------KRRISDLEDEILELMERIEELEEELAELEA-----------------ELAELEAELEE 142
|
170 180 190
....*....|....*....|....*....|....*..
gi 767931431 492 KTNQMAATIKQLEQRL--RQAERSRQSAELDNRLFKQ 526
Cdd:COG1579 143 KKAELDEELAELEAELeeLEAEREELAAKIPPELLAL 179
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
392-562 |
1.44e-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: 41.29 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 392 KQDRTAEGQALSEARKHLKEETQLRLDVEKEL---EMQIS----MRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRAL 464
Cdd:COG4942 26 EAELEQLQQEIAELEKELAALKKEEKALLKQLaalERRIAalarRIRALEQELAALEAELAELEKEIAELRAELEAQKEE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 465 KHELAFKLQSSDLGVKQKSELNSRLEEKTNQMAATIKQL-EQRLRQAERSRQSAELDNRLfKQDFGDKINSLQLEVEELT 543
Cdd:COG4942 106 LAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLaPARREQAEELRADLAELAAL-RAELEAERAELEALLAELE 184
|
170
....*....|....*....
gi 767931431 544 RQRNQLElELKQEKERRLQ 562
Cdd:COG4942 185 EERAALE-ALKAERQKLLA 202
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
351-550 |
1.48e-03 |
|
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: 41.75 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 351 SNTKLTEELAVANNriiTLQEEMERVKEESSYILESNRKGPKQDRtaegqALSEARKHLK--EETQLRLDVEKElemqis 428
Cdd:pfam12128 598 SEEELRERLDKAEE---ALQSAREKQAAAEEQLVQANGELEKASR-----EETFARTALKnaRLDLRRLFDEKQ------ 663
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 429 mrqemELAMKmLEKDVCEKQDALVSLRQQLD-DLRALKHEL-----AFKLQSSDLGVKQKSELNSRLEEKTNQMAAtIKQ 502
Cdd:pfam12128 664 -----SEKDK-KNKALAERKDSANERLNSLEaQLKQLDKKHqawleEQKEQKREARTEKQAYWQVVEGALDAQLAL-LKA 736
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 767931431 503 LEQRLRQAERSRQSA---ELDNRLFKQDF-GDKINSLQLEVEELTRQRNQLE 550
Cdd:pfam12128 737 AIAARRSGAKAELKAletWYKRDLASLGVdPDVIAKLKREIRTLERKIERIA 788
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
316-506 |
1.54e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 316 QITAILDQKNYVEELNRHLNAtvnnlQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEEssyiLESNRkgpKQDR 395
Cdd:COG4913 266 AARERLAELEYLRAALRLWFA-----QRRLELLEAELEELRAELARLEAELERLEARLDALREE----LDELE---AQIR 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 396 TAEGQALSEARKHLKEETQLRLDVEKELEMQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKLQSs 475
Cdd:COG4913 334 GNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEA- 412
|
170 180 190
....*....|....*....|....*....|.
gi 767931431 476 dlgvkQKSELNSRLEEKTNQmaatIKQLEQR 506
Cdd:COG4913 413 -----ALRDLRRELRELEAE----IASLERR 434
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
3-100 |
1.72e-03 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 41.51 E-value: 1.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 3 ETPPPPTAGAESCSEEPARGGEWRPEEPRRAPAGGTDREGEAGPPPASPAGQSEPDSPVAAPFFlLYPGDGGAGFGVRPP 82
Cdd:PRK07764 679 AAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLP-PEPDDPPDPAGAPAQ 757
|
90
....*....|....*...
gi 767931431 83 PQQQRSWRTPPSPGSPLP 100
Cdd:PRK07764 758 PPPPPAPAPAAAPAAAPP 775
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
324-560 |
2.12e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.20 E-value: 2.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 324 KNYVEELNRHLNATvNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEE-------SSYILESNRKGPKQDRT 396
Cdd:PRK03918 175 KRRIERLEKFIKRT-ENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEvkeleelKEEIEELEKELESLEGS 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 397 AEG--QALSEARKHLkEETQLRLDVEKELEMQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKLQS 474
Cdd:PRK03918 254 KRKleEKIRELEERI-EELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKE 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 475 SDLGVKQKSELNSRLEEKTNQMAAtikqLEQRLRQAERSRQSAELDNRLFKQDFGDKINSLQLEVEELTRQRNQLELELK 554
Cdd:PRK03918 333 LEEKEERLEELKKKLKELEKRLEE----LEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEIS 408
|
....*.
gi 767931431 555 QEKERR 560
Cdd:PRK03918 409 KITARI 414
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
344-557 |
2.23e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 40.29 E-value: 2.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 344 KVDALEKSNTKLTEELAVANNriitlQEEMERVKEESSY--ILESNRKGPKQDRTAEGQALSEaRKHLKEETQlrlDVEK 421
Cdd:pfam00038 19 KVRFLEQQNKLLETKISELRQ-----KKGAEPSRLYSLYekEIEDLRRQLDTLTVERARLQLE-LDNLRLAAE---DFRQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 422 ELEMQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDdlrALKHELAF--------------KLQSSDLGVKQKSELNS 487
Cdd:pfam00038 90 KYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIE---SLKEELAFlkknheeevrelqaQVSDTQVNVEMDAARKL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 488 RLEEKTNQMAAtikQLEQrlrQAERSRQSAEldnRLFKQDF----------GDKINSLQLEVEELTRQRNQLELELKQEK 557
Cdd:pfam00038 167 DLTSALAEIRA---QYEE---IAAKNREEAE---EWYQSKLeelqqaaarnGDALRSAKEEITELRRTIQSLEIELQSLK 237
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
342-563 |
2.29e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 41.11 E-value: 2.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 342 QAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESSYI--LESNRKGPKQDRTAEGQALSEARKHLKEETQLRLDV 419
Cdd:TIGR00618 679 QLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFneIENASSSLGSDLAAREDALNQSLKELMHQARTVLKA 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 420 EKELEMQISMRQEMEL----AMKMLEKDVCEKQDALVSLRQQLDDLRA-----LKHELAFKLQSSDLGVKQKSELNSRLE 490
Cdd:TIGR00618 759 RTEAHFNNNEEVTAALqtgaELSHLAAEIQFFNRLREEDTHLLKTLEAeigqeIPSDEDILNLQCETLVQEEEQFLSRLE 838
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767931431 491 EKTNQMAATIKQLEQ----RLRQAERSRQSAELdNRLFKQDFGdkINSLQLEVEELTRQrnQLELELKQEKERRLQN 563
Cdd:TIGR00618 839 EKSATLGEITHQLLKyeecSKQLAQLTQEQAKI-IQLSDKLNG--INQIKIQFDGDALI--KFLHEITLYANVRLAN 910
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
453-576 |
2.58e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.27 E-value: 2.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 453 SLRQQLDDLRALKHELAFKLQSSDLGVKQKSELNSRLEEKTNQMAATIKQLEQRLRQAERSRQSAELDNRLFKQdFGDKI 532
Cdd:COG4372 32 QLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELES-LQEEA 110
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 767931431 533 NSLQLEVEELTRQRNQLELELKQEKERRLQNDRSIPGRGSQKSE 576
Cdd:COG4372 111 EELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKE 154
|
|
| ATP_synt_b |
TIGR01144 |
ATP synthase, F0 subunit b; This model describes the F1/F0 ATP synthase b subunit in bacteria ... |
345-448 |
2.75e-03 |
|
ATP synthase, F0 subunit b; This model describes the F1/F0 ATP synthase b subunit in bacteria only. Scoring just below the trusted cutoff are the N-terminal domains of Mycobacterial b/delta fusion proteins and a subunit from an archaeon, Methanosarcina barkeri, in which the ATP synthase homolog differs in architecture and is not experimentally confirmed. This model helps resolve b from the related b' subunit. Within the family is an example from a sodium-translocating rather than proton-translocating ATP synthase. [Energy metabolism, ATP-proton motive force interconversion]
Pssm-ID: 130214 [Multi-domain] Cd Length: 147 Bit Score: 38.54 E-value: 2.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 345 VDALEKSNtkltEELAVANNRIitlQEEMERVKEESSYILE-SNRKGPKQDRTAEGQALSEARKhLKEETQLRLDVEKEl 423
Cdd:TIGR01144 35 LASAERAK----KEAALAQKKA---QVILKEAKDEAQEIIEnANKRGSEILEEAKAEAREEREK-IKAQARAEIEAEKE- 105
|
90 100 110
....*....|....*....|....*....|
gi 767931431 424 EMQISMRQE-----MELAMKMLEKDVCEKQ 448
Cdd:TIGR01144 106 QAREELRKQvadlsVLGAEKIIERNIDKQA 135
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
2-100 |
2.80e-03 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 40.74 E-value: 2.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 2 AETPPPPTAGAESCSEEPARGGewrpeePRRAPAGGTDREGEAGPPPASPAGQSEPDSPVAAPFFLLYPGDGGAGFGVRP 81
Cdd:PRK07764 393 APAAAAPSAAAAAPAAAPAPAA------AAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQP 466
|
90
....*....|....*....
gi 767931431 82 PPQQQRSWRTPPSPGSPLP 100
Cdd:PRK07764 467 APAPAAAPEPTAAPAPAPP 485
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
316-557 |
2.84e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 39.89 E-value: 2.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 316 QITAILDQKNYVEELNRHLNATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESSYILESNR------- 388
Cdd:COG1340 16 KIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNelreeld 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 389 --KGPKQDRTAEGQALSEARKHLKEE------TQLRLDVEKELEMQIS-MRQEMELAMKMLE--KDVCEKQDALVSLRQQ 457
Cdd:COG1340 96 elRKELAELNKAGGSIDKLRKEIERLewrqqtEVLSPEEEKELVEKIKeLEKELEKAKKALEknEKLKELRAELKELRKE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 458 LDDLRALKHELAFKLQS-SDLGVKQKSELNSrLEEKTNQMAATIKQLeqrlrQAERSRQSAELDNRLFK-QDFGDKINSL 535
Cdd:COG1340 176 AEEIHKKIKELAEEAQElHEEMIELYKEADE-LRKEADELHKEIVEA-----QEKADELHEEIIELQKElRELRKELKKL 249
|
250 260
....*....|....*....|..
gi 767931431 536 QLEVEELTRQRNQLELELKQEK 557
Cdd:COG1340 250 RKKQRALKREKEKEELEEKAEE 271
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
335-546 |
2.97e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.67 E-value: 2.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 335 NATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEE---SSYILESNRKGPKQDRTAEGQAL------SEA 405
Cdd:COG4913 684 SDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEEldeLQDRLEAAEDLARLELRALLEERfaaalgDAV 763
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 406 RKHLKEETQLRLDVEKELEMQIsmRQEMELAM-KMLEKDVCEKQDALVSL------RQQLDDLRAL---KHELAFKLQSS 475
Cdd:COG4913 764 ERELRENLEERIDALRARLNRA--EEELERAMrAFNREWPAETADLDADLeslpeyLALLDRLEEDglpEYEERFKELLN 841
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 476 DLGVKQKSELNSRLEEKTNQMAATIKQLEQRLRQAE-----------RSRQSAELdnRLFKQDFGDKINSLQLEVEELTR 544
Cdd:COG4913 842 ENSIEFVADLLSKLRRAIREIKERIDPLNDSLKRIPfgpgrylrleaRPRPDPEV--REFRQELRAVTSGASLFDEELSE 919
|
..
gi 767931431 545 QR 546
Cdd:COG4913 920 AR 921
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
2-100 |
3.41e-03 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 40.35 E-value: 3.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 2 AETPPPPTAGAESCSEEPARGGEWRPEEPRRAPAGGTDREGEAGPPPASPAGQSEPDSPVAAPFFLLYPGDGGA---GFG 78
Cdd:PRK07764 616 AAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAApaaPAG 695
|
90 100
....*....|....*....|..
gi 767931431 79 VRPPPQQQRSWRTPPSPGSPLP 100
Cdd:PRK07764 696 AAPAQPAPAPAATPPAGQADDP 717
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
327-561 |
4.04e-03 |
|
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: 40.00 E-value: 4.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 327 VEELNRHLNATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMervkeessYILESNRKGPKQDRTAEGQALSEAR 406
Cdd:TIGR04523 403 QEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQD--------SVKELIIKNLDNTRESLETQLKVLS 474
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 407 KHLKEETQLRLDVEKELEMQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKLQS--SDLgVKQKSE 484
Cdd:TIGR04523 475 RSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDleDEL-NKDDFE 553
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 485 LN-SRLEEKTNQMAATIKQLEQRLRQAERSRQsaELDNRLfkQDFGDKINSLQLEVEELTRQRNQLELELK--QEKERRL 561
Cdd:TIGR04523 554 LKkENLEKEIDEKNKEIEELKQTQKSLKKKQE--EKQELI--DQKEKEKKDLIKEIEEKEKKISSLEKELEkaKKENEKL 629
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
370-567 |
5.29e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.12 E-value: 5.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 370 QEEMERVKEESSYILESNRKGPKQDRTAEGQALSEARKHLKEETQLRLDVEKELEMQISMRQEMELAMKMLEkdvcEKQD 449
Cdd:PTZ00121 1614 KAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEE----DEKK 1689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 450 ALVSLRQQLDDLRalKHELAFKLQSSDlgVKQKSELNSRLEEKTNQMAATIKQLEQRLRQAERSRQSAELDNRL--FKQD 527
Cdd:PTZ00121 1690 AAEALKKEAEEAK--KAEELKKKEAEE--KKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIahLKKE 1765
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 767931431 528 FGDKINSLQLEVEELtrqrnqLELELKQEKE-RRLQNDRSI 567
Cdd:PTZ00121 1766 EEKKAEEIRKEKEAV------IEEELDEEDEkRRMEVDKKI 1800
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
394-559 |
5.42e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 39.92 E-value: 5.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 394 DRTAEGQALSEARKHLKEETQLRLDVEKELEMQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKLQ 473
Cdd:COG1196 624 GRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEE 703
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 474 SSDLGVKQKSELNSRLEEKTNQMAATIKQLEQRLRQAERSRQSAELDNRLFKQDFGDKINSLQLEVEELTRQRNQL---- 549
Cdd:COG1196 704 EEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALgpvn 783
|
170
....*....|...
gi 767931431 550 ---ELELKQEKER 559
Cdd:COG1196 784 llaIEEYEELEER 796
|
|
| PHA03378 |
PHA03378 |
EBNA-3B; Provisional |
2-98 |
5.43e-03 |
|
EBNA-3B; Provisional
Pssm-ID: 223065 [Multi-domain] Cd Length: 991 Bit Score: 39.67 E-value: 5.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 2 AETPPPPTAGAESCSEEPaRGGEWRPEEPRRAPAGGTDREGEAGPPPASPAGQSEPDSPVAAPFFLLYPGDGGAGFGVRP 81
Cdd:PHA03378 700 APTPMRPPAAPPGRAQRP-AAATGRARPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAAAPGAPTPQP 778
|
90 100
....*....|....*....|..
gi 767931431 82 PPQ-----QQRSwRTPPSPGSP 98
Cdd:PHA03378 779 PPQappapQQRP-RGAPTPQPP 799
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
328-562 |
5.77e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 39.64 E-value: 5.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 328 EELNRhLNATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESSY------ILESNRKGPKQDRTAEGQA 401
Cdd:PRK02224 251 EELET-LEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLddadaeAVEARREELEDRDEELRDR 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 402 LSEAR----KHLKEETQLR---LDVEKELEMQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRAlkhelAFKLQS 474
Cdd:PRK02224 330 LEECRvaaqAHNEEAESLRedaDDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRE-----RFGDAP 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 475 SDLGVKQ--KSELNSRLEEKTNQMA---ATIKQLEQRLRQAER----------------SRQSAELDNRlfkqdfGDKIN 533
Cdd:PRK02224 405 VDLGNAEdfLEELREERDELREREAeleATLRTARERVEEAEAlleagkcpecgqpvegSPHVETIEED------RERVE 478
|
250 260 270
....*....|....*....|....*....|....
gi 767931431 534 SLQLEVEELTRQRNQLE-----LELKQEKERRLQ 562
Cdd:PRK02224 479 ELEAELEDLEEEVEEVEerlerAEDLVEAEDRIE 512
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
342-565 |
5.77e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 39.89 E-value: 5.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 342 QAKVDALEKSNTKLTEELAvannriitLQEEMErvkeessyILESNrkgpkqdrtaegqaLSEARKHLKEETQLRLDVEK 421
Cdd:PLN02939 149 QARLQALEDLEKILTEKEA--------LQGKIN--------ILEMR--------------LSETDARIKLAAQEKIHVEI 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 422 ELEMQISMRQEMELAMKMLEKDVCEKQDALVSLRQQ----LDDLRALKHELafklqssdLGVKQKSELNSRLEEKTNQMA 497
Cdd:PLN02939 199 LEEQLEKLRNELLIRGATEGLCVHSLSKELDVLKEEnmllKDDIQFLKAEL--------IEVAETEERVFKLEKERSLLD 270
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767931431 498 ATIKQLEQRLRQAersrQSAELDNRLFKQD-FGDKINSLQLEVEELTRQRNQLELELKQEKERRLQNDR 565
Cdd:PLN02939 271 ASLRELESKFIVA----QEDVSKLSPLQYDcWWEKVENLQDLLDRATNQVEKAALVLDQNQDLRDKVDK 335
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
321-565 |
5.98e-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: 39.77 E-value: 5.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 321 LDQKNYVEELNRHLNATVNNLQAKVDA-------LEKSNTKLTEELAVANNRIITLQEEMErVKEESSYILESNRKGPK- 392
Cdd:pfam01576 649 LEAKEELERTNKQLRAEMEDLVSSKDDvgknvheLERSKRALEQQVEEMKTQLEELEDELQ-ATEDAKLRLEVNMQALKa 727
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 393 ---QDRTAEGQALSEARKHLKEetQLRlDVEKELEMQISMRQEMELAMKMLEKDVCE-----------KQDALVSLRQQL 458
Cdd:pfam01576 728 qfeRDLQARDEQGEEKRRQLVK--QVR-ELEAELEDERKQRAQAVAAKKKLELDLKEleaqidaankgREEAVKQLKKLQ 804
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 459 DDLRALKHELAFKLQSSDLGVKQKSELnsrlEEKTNQMAATIKQLEQRLRQAERSRQSAELDnrlfKQDFGDKINS---- 534
Cdd:pfam01576 805 AQMKDLQRELEEARASRDEILAQSKES----EKKLKNLEAELLQLQEDLAASERARRQAQQE----RDELADEIASgasg 876
|
250 260 270
....*....|....*....|....*....|....*
gi 767931431 535 ---LQLEVEELTRQRNQLELELKQEKER-RLQNDR 565
Cdd:pfam01576 877 ksaLQDEKRRLEARIAQLEEELEEEQSNtELLNDR 911
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
323-560 |
7.31e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 39.23 E-value: 7.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 323 QKNYVEELNRHLNATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMErvkeessyilesnrkgpkqDRTAEGQAL 402
Cdd:PHA02562 200 YNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIE-------------------DPSAALNKL 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 403 SEARKHLKEETQLrldVEKELEM------------QISMRQEMelamkmlekdVCEKQDALVSLRQQLDDLRALKHELAF 470
Cdd:PHA02562 261 NTAAAKIKSKIEQ---FQKVIKMyekggvcptctqQISEGPDR----------ITKIKDKLKELQHSLEKLDTAIDELEE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 471 KLQSSDLGVKQKSELNSRLEEKTNQMAATIKQLEQrlRQAERSRQSAEldnrlfKQDFGDKINSLQLEVEELTRQRNqle 550
Cdd:PHA02562 328 IMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKK--VKAAIEELQAE------FVDNAEELAKLQDELDKIVKTKS--- 396
|
250
....*....|
gi 767931431 551 lELKQEKERR 560
Cdd:PHA02562 397 -ELVKEKYHR 405
|
|
| DUF6264 |
pfam19779 |
Family of unknown function (DUF6264); This family of putative integral membrane proteins is ... |
23-106 |
8.17e-03 |
|
Family of unknown function (DUF6264); This family of putative integral membrane proteins is functionally uncharacterized. This family of proteins is found in bacteria. Proteins in this family are typically between 179 and 218 amino acids in length.
Pssm-ID: 466182 Cd Length: 182 Bit Score: 37.63 E-value: 8.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 23 GEWRPEEPRRAPAGGTDREGEAGPPPASPAGQSEPDS-PVAAPffllyPGDGGAGFGVRPPPQQQRswrtPPSPG-SPLP 100
Cdd:pfam19779 5 GEYAPPGWQRAPIGDPAAAAAAAPPAAPAPAAPAPPAaPAAPP-----AAPPPPGAPAPGAPAAAR----RARRWdRIAT 75
|
....*.
gi 767931431 101 FLLLSY 106
Cdd:pfam19779 76 IALLVF 81
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
485-573 |
8.35e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 39.23 E-value: 8.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 485 LNSRLEEKTNQMAATIKQLEQRLRQAErsRQSAELDNRL--FKQ-----DFGDKINSLQLEVEELTRQRNQLELELkQEK 557
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELR--KELEEAEAALeeFRQknglvDLSEEAKLLLQQLSELESQLAEARAEL-AEA 238
|
90
....*....|....*.
gi 767931431 558 ERRLQNDRSIPGRGSQ 573
Cdd:COG3206 239 EARLAALRAQLGSGPD 254
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
2-98 |
8.91e-03 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 39.20 E-value: 8.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 2 AETPPPPTAGAESCSEEPARGGEWRPEEPRRAPAGGTDREGEAGPPPASPAGQSEPDSPVAAPFFLLYPGDGGAGFGVRP 81
Cdd:PRK07764 398 APSAAAAAPAAAPAPAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPAPAPAAAPEPT 477
|
90
....*....|....*..
gi 767931431 82 PPQQQRSWRTPPSPGSP 98
Cdd:PRK07764 478 AAPAPAPPAAPAPAAAP 494
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
415-542 |
9.04e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 38.46 E-value: 9.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767931431 415 LRLDVEKELEmqiSMRQEMELAMKMLEK------DVCEKQDALVSLRQQL------------DDLRALKHELAFKLQSSD 476
Cdd:smart00787 145 LKEGLDENLE---GLKEDYKLLMKELELlnsikpKLRDRKDALEEELRQLkqledeledcdpTELDRAKEKLKKLLQEIM 221
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767931431 477 LGVK-------QKSELNSRLEEKTNQmaatIKQLEQRLRQAERSRqsaeLDNRLFkqDFgDKINSLQLEVEEL 542
Cdd:smart00787 222 IKVKkleeleeELQELESKIEDLTNK----KSELNTEIAEAEKKL----EQCRGF--TF-KEIEKLKEQLKLL 283
|
|
| |
